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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.

Chemistry databases

SwissLipidsiSLP:000001349.

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001930631 – 520Bile acid-coenzyme A ligaseAdd BLAST520

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi411468.CLOSCI_03136.

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 42Combined sources11
Beta strandi46 – 52Combined sources7
Beta strandi58 – 62Combined sources5
Helixi63 – 79Combined sources17
Beta strandi87 – 90Combined sources4
Helixi96 – 107Combined sources12
Beta strandi111 – 114Combined sources4
Helixi121 – 131Combined sources11
Beta strandi134 – 137Combined sources4
Helixi153 – 158Combined sources6
Beta strandi175 – 179Combined sources5
Beta strandi187 – 191Combined sources5
Helixi199 – 209Combined sources11
Beta strandi217 – 219Combined sources3
Helixi226 – 237Combined sources12
Beta strandi242 – 246Combined sources5
Helixi250 – 259Combined sources10
Beta strandi264 – 267Combined sources4
Helixi269 – 277Combined sources9
Helixi283 – 286Combined sources4
Beta strandi290 – 294Combined sources5
Helixi301 – 311Combined sources11
Helixi313 – 315Combined sources3
Beta strandi316 – 321Combined sources6
Helixi323 – 325Combined sources3
Beta strandi328 – 332Combined sources5
Helixi333 – 338Combined sources6
Beta strandi344 – 347Combined sources4
Beta strandi352 – 355Combined sources4
Beta strandi368 – 372Combined sources5
Helixi376 – 379Combined sources4
Beta strandi381 – 383Combined sources3
Turni393 – 395Combined sources3
Beta strandi402 – 405Combined sources4
Beta strandi411 – 413Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LGCX-ray2.19A1-520[»]
ProteinModelPortaliP19409.
SMRiP19409.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4LGCX-ray2.19A1-520[»]
ProteinModelPortaliP19409.
SMRiP19409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi411468.CLOSCI_03136.

Chemistry databases

SwissLipidsiSLP:000001349.

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...

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: November 2, 2016
This is version 70 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.