KEGG ENZYME: 6.2.1.50

ENZYME: 6.2.1.50

Entry

EC 6.2.1.50                 Enzyme

Name

4-hydroxybenzoate adenylyltransferase FadD22;
fadD22 (gene name);
4-hydroxybenzoate adenylase

Class

Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases

Sysname

4-hydroxybenzoate:holo-[4-hydroxyphenylalkanoate synthase] ligase (AMP-forming)

Reaction(IUBMB)

ATP + 4-hydroxybenzoate + holo-[4-hydroxyphenylalkanoate synthase] = AMP + diphosphate + 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase] (overall reaction);
(1a) ATP + 4-hydroxybenzoate = 4-hydroxybenzoyl-adenylate + diphosphate [RN:R11608];
(1b) 4-hydroxybenzoyl-adenylate + holo-[4-hydroxyphenylalkanoate synthase] = AMP + 4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase]

Reaction(KEGG)

R11608;
(other) R11872 R11873

Substrate

ATP [CPD:C00002];
4-hydroxybenzoate [CPD:C00156];
holo-[4-hydroxyphenylalkanoate synthase];
4-hydroxybenzoyl-adenylate [CPD:C21497]

Product

AMP [CPD:C00020];
diphosphate [CPD:C00013];
4-hydroxybenzoyl-[4-hydroxyphenylalkanoate synthase];
4-hydroxybenzoyl-adenylate [CPD:C21497]

Comment

This mycobacterial enzyme participates in the biosynthesis of phenolphthiocerols. Following the substrate's activation by adenylation, it is transferred to an acyl-carrier protein domain within the enzyme, from which it is transferred to EC 2.3.1.261, 4-hydroxyphenylalkanoate synthase.

History

EC 6.2.1.50 created 2017 as EC 2.7.7.98, transferred 2017 to EC 6.2.1.50

Orthology

K12424

4-hydroxybenzoate adenylyltransferase

Genes

MTU:	Rv2948c(fadD22)

MTV:	RVBD_2948c

MTC:

MT3021

MRA:	MRA_2975(fadD22)

MTF:	TBFG_12962

MTB:	TBMG_01023

MTK:	TBSG_01031

MTZ:	TBXG_001013

MTG:	MRGA327_18125

MTI:	MRGA423_18315

MTE:	CCDC5079_2708

MTUR:

CFBS_3107(fadD22)

MTL:	CCDC5180_2672

MTO:	MTCTRI2_3006(fadD22)

MTD:	UDA_2948c(fadD22)

MTN:	ERDMAN_3231(fadD22)

MTJ:	J112_15780

MTUB:

MT7199_2983

MTUC:

J113_20530

MTUE:

J114_15745

MTX:	M943_15185

MTUH:

I917_20710

MTUL:

TBHG_02878

MTUT:

HKBT1_3094(fadD22)

MTUU:

HKBT2_3099(fadD22)

MTQ:	HKBS1_3101(fadD22)

MBO:	BQ2027_MB2972C(fadD22)

MBB:	BCG_2969c(fadD22)

MBT:	JTY_2964(fadD22)

MBM:	BCGMEX_2964c(fadD22)

MBK:	K60_030540

MBX:

BCGT_2785

MAF:	MAF_29530(fadD22)

MMIC:

RN08_3250

MCE:	MCAN_29681(fadD22)

MCQ:	BN44_60423(fadD)

MCV:	BN43_40655(fadD)

MCX:	BN42_40947(fadD)

MCZ:	BN45_51359(fadD)

MORY:

MO_003079

MLE:	ML0134(fadD22)

MLB:	MLBr00134(fadD22)

MUL:	MUL_2004(fadD22)

MMI:	MMAR_1761(fadD22)

MMAE:

MMARE11_16800(fadD22)

MLI:	MULP_01916(fadD22)

MPSE:

MPSD_40750(fadD22)

MSHO:

MSHO_54820(fadD22)

MKN:	MKAN_23940

MHAD:

B586_03305

MBAI:

MB901379_01576

MLJ:	MLAC_28860(fadD22)

MSHJ:

MSHI_07220(fadD22)

MOT:	LTS72_16050

MLM:	MLPF_0162(fadD22)

MAUB:

MAUB_36910(fadD22)

SCB:

SCAB_8391

SVL:	Strvi_3914

SRC:	M271_05895

SXI:	SXIM_01890(ximA)

STRM:

M444_36455 M444_37810

STSI:

A4E84_25000

STIR:

DDW44_31240

SHAW:

CEB94_25390

SPHV:

F9278_43570

SCOE:

CP976_26830

SSPB:

CP982_00250

SGK:	PET44_33895 PET44_35080

SCT:

SCAT_5491

SCY:	SCATT_54890

THAO:

NI17_019195

NDA:

Ndas_1765

SRO:

Sros_3763

SEN:

SACE_4037

AMYB:

BKN51_40540

PHH:	AFB00_14380

APRE:

CNX65_18010

AMI:

Amir_3554

SESP:

BN6_22800 BN6_35920

SSYI:

EKG83_31190

KPHY:

AOZ06_18880

PLK:	CIK06_25340

» show all

Reference

1 [PMID:20553505]

Authors

Simeone R, Leger M, Constant P, Malaga W, Marrakchi H, Daffe M, Guilhot C, Chalut C

Title

Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis.

Journal

FEBS J 277:2715-25 (2010)
DOI:10.1111/j.1742-464X.2010.07688.x

Sequence

[mtu:Rv2948c]

Reference

2 [PMID:25561717]

Authors

Vergnolle O, Chavadi SS, Edupuganti UR, Mohandas P, Chan C, Zeng J, Kopylov M, Angelo NG, Warren JD, Soll CE, Quadri LE

Title

Biosynthesis of cell envelope-associated phenolic glycolipids in Mycobacterium marinum.

Journal

J Bacteriol 197:1040-50 (2015)
DOI:10.1128/JB.02546-14

Sequence

[mmi:MMAR_1761]

Other DBs

ExplorEnz - The Enzyme Database:

6.2.1.50

IUBMB Enzyme Nomenclature:

6.2.1.50

ExPASy - ENZYME nomenclature database:

6.2.1.50

BRENDA, the Enzyme Database:

6.2.1.50

All links

Chemical substance (7)   
   KEGG COMPOUND (7)   
Chemical reaction (3)   
   KEGG REACTION (3)   
Gene (86)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (85)   
Protein sequence (8)   
   UniProt (4)   
   SWISS-PROT (4)   
DNA sequence (2)   
   GenBank (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (7)   
All databases (113)   

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