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Protein

Bile acid-coenzyme A ligase

Gene

baiB

Organism
Clostridium scindens (strain JCM 10418 / VPI 12708)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Active with a large number of C-24 bile acids possessing unhindered C-24 carboxyl groups. Requires ATP and produces AMP and pyrophosphate in addition to the bile-acid CoA thioester.1 Publication

Pathwayi: bile acid degradation

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:BAIBEUBSP-MONOMER.
UniPathwayiUPA00279.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile acid-coenzyme A ligase (EC:6.-.-.-)
Gene namesi
Name:baiB
OrganismiClostridium scindens (strain JCM 10418 / VPI 12708)
Taxonomic identifieri29347 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesLachnospiraceae

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Bile acid-coenzyme A ligasePRO_0000193063Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi411468.CLOSCI_03136.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 4211Combined sources
Beta strandi46 – 527Combined sources
Beta strandi58 – 625Combined sources
Helixi63 – 7917Combined sources
Beta strandi87 – 904Combined sources
Helixi96 – 10712Combined sources
Beta strandi111 – 1144Combined sources
Helixi121 – 13111Combined sources
Beta strandi134 – 1374Combined sources
Helixi153 – 1586Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi187 – 1915Combined sources
Helixi199 – 20911Combined sources
Beta strandi217 – 2193Combined sources
Helixi226 – 23712Combined sources
Beta strandi242 – 2465Combined sources
Helixi250 – 25910Combined sources
Beta strandi264 – 2674Combined sources
Helixi269 – 2779Combined sources
Helixi283 – 2864Combined sources
Beta strandi290 – 2945Combined sources
Helixi301 – 31111Combined sources
Helixi313 – 3153Combined sources
Beta strandi316 – 3216Combined sources
Helixi323 – 3253Combined sources
Beta strandi328 – 3325Combined sources
Helixi333 – 3386Combined sources
Beta strandi344 – 3474Combined sources
Beta strandi352 – 3554Combined sources
Beta strandi368 – 3725Combined sources
Helixi376 – 3794Combined sources
Beta strandi381 – 3833Combined sources
Turni393 – 3953Combined sources
Beta strandi402 – 4054Combined sources
Beta strandi411 – 4133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LGCX-ray2.19A1-520[»]
ProteinModelPortaliP19409.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
KOiK15868.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19409-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHKKSACERE GKELKRDFFN KFNLGTSNFV TPGKQLEYVS ECKPDSTAVI
60 70 80 90 100
CLDKEQNCSV ITWHQLHVYS SQLAWYLIEN EIGPGSIVLT MFPNSIEHII
110 120 130 140 150
AVFAIWKAGA CYMPMSYKAA ESEIREACDT IHPNAAFAEC KIPGLKFCLS
160 170 180 190 200
ADEIYEAMEG RSKEMPSDRL ANPNMISLSG GTSGKMKFIR QNLPCGLDDE
210 220 230 240 250
TIRSWSLMSG MGFEQRQLLV GPLFHGAPHS AAFNGLFMGN TLVLTRNLCP
260 270 280 290 300
GNILNMIKKY KIEFIQMVPT LMNRLAKLEG VGKEDFASLK ALCHTGGVCS
310 320 330 340 350
PWLKQIWIDL LGPEKIYEMY SMTECIGLTC IRGDEWVKHP GSIGRPVGDS
360 370 380 390 400
KVSIRDENGK EVAPFEIGEI YMTAPASYLV TEYINWEPLE VKEGGFRSVG
410 420 430 440 450
DIGYVDEQGY LYFSDRRSDM LVSGGENVFA TEVETALLRY KDILDAVVVG
460 470 480 490 500
IPDEDLGRRL HAVIETGKEI PAEELKTFLR KYLTPYKIPK TFEFVRSIRR
510 520
GDNGKADRKR ILEDCIARGG
Length:520
Mass (Da):58,294
Last modified:November 1, 1990 - v1
Checksum:i871254FDF6852CC4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57489 Genomic DNA. Translation: AAC45410.1.

Genome annotation databases

KEGGiag:AAC45410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57489 Genomic DNA. Translation: AAC45410.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LGCX-ray2.19A1-520[»]
ProteinModelPortaliP19409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi411468.CLOSCI_03136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC45410.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
KOiK15868.

Enzyme and pathway databases

UniPathwayiUPA00279.
BioCyciMetaCyc:BAIBEUBSP-MONOMER.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708."
    Mallonee D.H., White W.B., Hylemon P.B.
    J. Bacteriol. 172:7011-7019(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase."
    Mallonee D.H., Adams J.L., Hylemon P.B.
    J. Bacteriol. 174:2065-2071(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiBAIB_CLOSV
AccessioniPrimary (citable) accession number: P19409
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 8, 2016
This is version 69 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

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.