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Protein

p-hydroxybenzoic acid--AMP ligase FadD22

Gene

fadD22

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in a CoA-independent manner by attack of the phosphopantetheine thiol of FadD22. This intermediate primes the biosynthesis of the phenolphthiocerol (PPOL) by presenting the pHBA starter unit for elongation by Pks15/1. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B).1 Publication

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • ligase activity Source: UniProtKB
  • phosphopantetheine binding Source: InterPro

GO - Biological processi

  • Actinobacterium-type cell wall biogenesis Source: UniProtKB
  • fatty acid biosynthetic process Source: UniProtKB-UniPathway
  • lipid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
p-hydroxybenzoic acid--AMP ligase FadD22 (EC:6.2.1.-)
Short name:
p-HB--AMP ligase FadD22
Alternative name(s):
p-hydroxybenzoic acid-AMP synthetase
Short name:
p-HB-AMP synthetase
Gene namesi
Name:fadD22
Ordered Locus Names:MMAR_1761
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi576S → A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004063521 – 702p-hydroxybenzoic acid--AMP ligase FadD22Add BLAST702

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei576O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi216594.MMAR_1761.

Structurei

3D structure databases

ProteinModelPortaliB2HIL6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini543 – 613Acyl carrierPROSITE-ProRule annotationAdd BLAST71

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000047054.
KOiK12424.
OMAiPRNDNGK.
OrthoDBiPOG091H02SZ.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
InterProiIPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2HIL6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNENVAGLL AERASEAGWT DQPAYYAPDV VTHGQIHDGA ARLGAVLANR
60 70 80 90 100
GLCRGDRVLL CMPDSPELVQ VLLACLARGI LAFLANPELH RDDHAFQERD
110 120 130 140 150
TQAALVITSG PLCDRFAPST VVDAADLFSE AARVGPADYE ILGGDAAAYA
160 170 180 190 200
TYTSGTTGPP KAAIHRHCDV FAFVEAMCRN ALRLTPADIG LSSARMYFAY
210 220 230 240 250
GLGNSVWFPL ATGSSAVVNP LPVGAEVAAT LSARFEPSVL YGVPNFFARV
260 270 280 290 300
VDACSADSFR SVRCVVSAGE ALEVGLAERL TEFFGGIPIL DGVGSTEVGQ
310 320 330 340 350
TFVSNTVDEW RPGSLGKVLP PYQIRVVAPD GAAAGPGVEG DLWVRGPSIA
360 370 380 390 400
ESYWNWPEPL LTDEGWLDTR DRVCIDDDGW VTYACRADDT EIVGAVNINP
410 420 430 440 450
REIERLIVEE DAVAEVAVVG VKEATGASTL QAFLVPASAE GIDGSVMRDI
460 470 480 490 500
HRRLLTRLSA FKVPHRFAVV ERLPRTANGK LLRSALRGQT PAKPIWELAS
510 520 530 540 550
AEHRSGAPGQ LDDQSASALV SGSREVSLKE RLAALQQERH RLVLDAVCGE
560 570 580 590 600
TAKMLGEPDP RSVNRDLAFS ELGFDSQMTV ELCHRLAAAT GLRVPETVGW
610 620 630 640 650
DYGSISGLAQ YLEAELSGAD RRVTPQSARS GARALPLIEA QLNKVEELTA
660 670 680 690 700
AIADGEKPRV AERLRALLGT ITEGQEHWGQ RIAAASTPDE IFQLIDSEFG

ES
Length:702
Mass (Da):75,181
Last modified:June 10, 2008 - v1
Checksum:iAFAAFC5996F683F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40210.1.
RefSeqiWP_012393569.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC40210; ACC40210; MMAR_1761.
KEGGimmi:MMAR_1761.
PATRICi18064395. VBIMycMar75906_1882.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40210.1.
RefSeqiWP_012393569.1. NC_010612.1.

3D structure databases

ProteinModelPortaliB2HIL6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_1761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC40210; ACC40210; MMAR_1761.
KEGGimmi:MMAR_1761.
PATRICi18064395. VBIMycMar75906_1882.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000047054.
KOiK12424.
OMAiPRNDNGK.
OrthoDBiPOG091H02SZ.

Enzyme and pathway databases

UniPathwayiUPA00094.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
InterProiIPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFAA22_MYCMM
AccessioniPrimary (citable) accession number: B2HIL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 10, 2008
Last modified: November 2, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.