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P19337

- BAIA2_CLOSV

UniProt

P19337 - BAIA2_CLOSV

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Protein

Bile acid 7-dehydroxylase 2

Gene

baiA2

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

Functioni

7-alpha-dehydroxylation of cholic acid and chenodeoxycholate, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid.

Catalytic activityi

Deoxycholate + FAD + H2O = cholate + FADH2.
Lithocholate + FAD + H2O = chenodeoxycholate + FADH2.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441SubstrateBy similarity
Active sitei157 – 1571Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 137NADSequence Analysis
Nucleotide bindingi32 – 365NADSequence Analysis

GO - Molecular functioni

  1. bile-acid 7alpha-dehydroxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. bile acid catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:BAIA2EUBSP-MONOMER.
UniPathwayiUPA00279.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile acid 7-dehydroxylase 2 (EC:1.17.99.5)
Alternative name(s):
Bile acid-inducible protein 2
Cholate 7-alpha-dehydroxylase 2
Gene namesi
Name:baiA2
OrganismiClostridium scindens (strain JCM 10418 / VPI 12708)
Taxonomic identifieri29347 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesLachnospiraceae

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Bile acid 7-dehydroxylase 2PRO_0000054525Add
BLAST

Expressioni

Inductioni

Presence of C(24) bile acids containing a 7-alpha-hydroxy group.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Beta strandi8 – 114Combined sources
Turni12 – 154Combined sources
Helixi17 – 2812Combined sources
Beta strandi32 – 365Combined sources
Helixi40 – 5314Combined sources
Beta strandi60 – 623Combined sources
Helixi69 – 8315Combined sources
Beta strandi88 – 914Combined sources
Helixi101 – 1033Combined sources
Helixi106 – 11611Combined sources
Helixi118 – 13114Combined sources
Turni132 – 1354Combined sources
Beta strandi137 – 1426Combined sources
Helixi146 – 1494Combined sources
Helixi160 – 17415Combined sources
Helixi176 – 1783Combined sources
Beta strandi180 – 1878Combined sources
Helixi193 – 1964Combined sources
Helixi200 – 20910Combined sources
Helixi218 – 22912Combined sources
Helixi231 – 2333Combined sources
Beta strandi238 – 2436Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IS2X-ray1.90A1-249[»]
4IS3X-ray2.00A/B/C/D1-249[»]
ProteinModelPortaliP19337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19337-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNLVQDKVTI ITGGTRGIGF AAAKIFIDNG AKVSIFGETQ EEVDTALAQL
60 70 80 90 100
KELYPEEEVL GFAPDLTSRD AVMAAVGQVA QKYGRLDVMI NNAGITSNNV
110 120 130 140 150
FSRVSEEEFK HIMDINVTGV FNGAWCAYQC MKDAKKGVII NTASVTGIFG
160 170 180 190 200
SLSGVGYPAS KASVIGLTHG LGREIIRKNI RVVGVAPGVV NTDMTNGNPP
210 220 230 240
EIMEGYLKAL PMKRMLEPEE IANVYLFLAS DLASGITATT VSVDGAYRP
Length:249
Mass (Da):26,538
Last modified:November 1, 1990 - v1
Checksum:i9A39B78BB63DC5AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22623 Genomic DNA. Translation: AAB61150.1.
U57489 Genomic DNA. Translation: AAC45414.1.
PIRiA31841.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22623 Genomic DNA. Translation: AAB61150.1 .
U57489 Genomic DNA. Translation: AAC45414.1 .
PIRi A31841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IS2 X-ray 1.90 A 1-249 [» ]
4IS3 X-ray 2.00 A/B/C/D 1-249 [» ]
ProteinModelPortali P19337.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00279 .
BioCyci MetaCyc:BAIA2EUBSP-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEi PS00061. ADH_SHORT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "Multiple copies of a bile acid-inducible gene in Eubacterium sp. strain VPI 12708."
    Gopal-Srivastava R., Mallonee D.H., White W.B., Hylemon P.B.
    J. Bacteriol. 172:4420-4426(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Evidence for a multigene family involved in bile acid 7-dehydroxylation in Eubacterium sp. strain VPI 12708."
    White W.B., Franklund C.V., Coleman J.P., Hylemon P.B.
    J. Bacteriol. 170:4555-4561(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiBAIA2_CLOSV
AccessioniPrimary (citable) accession number: P19337
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 26, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are three genes for BaiA proteins: baiA1 is identical to baiA3 and there is 81% identity with baiA2.

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

External Data

Dasty 3