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Protein

p-hydroxybenzoic acid--AMP ligase FadD22

Gene

fadD22

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed-Annotation score: Annotation score: 4 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

BioCyciMetaCyc:MONOMER-19623.
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:Mb2972c
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001419 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Disruption of fadD22 abolishes the production of phenolphthioceroL.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004063511 – 705p-hydroxybenzoic acid--AMP ligase FadD22Add BLAST705

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei579O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ7TXK7.
SMRiQ7TXK7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini546 – 616Acyl carrierPROSITE-ProRule annotationAdd BLAST71

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000047054.
KOiK12424.
OMAiFGLFAHY.

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.

Q7TXK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNGNLAGLL AEQASEAGWY DRPAFYAADV VTHGQIHDGA ARLGEVLRNR
60 70 80 90 100
GLSSGDRVLL CLPDSPDLVQ LLLACLARGV MAFLANPELH RDDHALAARN
110 120 130 140 150
TEPALVVTSD ALRDRFQPSR VAEAAELMSE AARVAPGGYE PMGGDALAYA
160 170 180 190 200
TYTSGTTGPP KAAIHRHADP LTFVDAMCRK ALRLTPEDTG LCSARMYFAY
210 220 230 240 250
GLGNSVWFPL ATGGSAVINS APVTPEAAAI LSARFGPSVL YGVPNFFARV
260 270 280 290 300
IDSCSPDSFR SLRCVVSAGE ALELGLAERL MEFFGGIPIL DGIGSTEVGQ
310 320 330 340 350
TFVSNRVDEW RLGTLGRVLP PYEIRVVAPD GTTAGPGVEG DLWVRGPAIA
360 370 380 390 400
KGYWNRPDSP VANEGWLDTR DRVCIDSDGW VTYRCRADDT EVIGGVNVDP
410 420 430 440 450
REVERLIIED EAVAEAAVVA VRESTGASTL QAFLVATSGA TIDGSVMRDL
460 470 480 490 500
HRGLLNRLSA FKVPHRFAVV DRLPRTPNGK LVRGALRKQS PTKPIWELSL
510 520 530 540 550
TEPGSGVRAQ RDDLSASNMT IAGGNDGGAT LRERLVALRQ ERQRLVVDAV
560 570 580 590 600
CAEAAKMLGE PDPWSVDQDL AFSELGFDSQ MTVTLCKRLA AVTGLRLPET
610 620 630 640 650
VGWDYGSISG LAQYLEAELA GGHGRLKSAG PVNSGATGLW AIEEQLNKVE
660 670 680 690 700
ELVAVIADGE KQRVADRLRA LLGTIAGSEA GLGKLIQAAS TPDEIFQLID

SELGK
Length:705
Mass (Da):75,198
Last modified:October 1, 2003 - v1
Checksum:i600F2D0EABFDF1DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44239.1.
RefSeqiNP_856617.1. NC_002945.3.
WP_003414884.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCDO44239; CDO44239; Mb2972c.
GeneIDi1092133.
KEGGimbo:Mb2972c.
PATRICi18008264. VBIMycBov88188_3264.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248333 Genomic DNA. Translation: CDO44239.1.
RefSeqiNP_856617.1. NC_002945.3.
WP_003414884.1. NC_002945.3.

3D structure databases

ProteinModelPortaliQ7TXK7.
SMRiQ7TXK7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCDO44239; CDO44239; Mb2972c.
GeneIDi1092133.
KEGGimbo:Mb2972c.
PATRICi18008264. VBIMycBov88188_3264.

Phylogenomic databases

HOGENOMiHOG000047054.
KOiK12424.
OMAiFGLFAHY.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:MONOMER-19623.

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_MYCBO
AccessioniPrimary (citable) accession number: Q7TXK7
Secondary accession number(s): X2BM70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 82 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

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.