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Protein

Bile acid 7-dehydroxylase 2

Gene

baiA2

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

Functioni

Catalyzes the conversion of the C3-hydroxy/oxo group of CoA conjugated bile acids. The preferred direction of reaction depends on the pH.1 Publication

Catalytic activityi

A 3-alpha-hydroxbile acid CoA ester + NAD+ = a 3-oxobile acid CoA ester + NADH.1 Publication

Cofactori

NAD+1 PublicationNote: Binds 1 NAD+ per subunit.1 Publication

Kineticsi

kcat is 10 min(-1) with cholyl-CoA as substrate. kcat is 12 min(-1) with chenodeoxycholyl-CoA as substrate. kcat is 11 min(-1) with litocholyl-CoA as substrate. kcat is 9.5 min(-1) with deoxycholyl-CoA as substrate. kcat is 8.3 min(-1) with 3-oxocholyl-CoA as substrate. kcat is 10 min(-1) with 3-oxochenodeoxycholyl-CoA as substrate. kcat is 7.3 min(-1) with 3-oxolitocholyl-CoA as substrate. kcat is 9.1 min(-1) with 3-oxodeoxycholyl-CoA as substrate.1 Publication

Manual assertion based on experiment ini

  1. KM=32 µM for cholyl-CoA1 Publication
  2. KM=23 µM for chenodeoxycholyl-CoA1 Publication
  3. KM=18 µM for litocholyl-CoA1 Publication
  4. KM=117 µM for deoxycholyl-CoA1 Publication
  5. KM=1.8 µM for 3-oxocholyl-CoA1 Publication
  6. KM=1.1 µM for 3-oxochenodeoxycholyl-CoA1 Publication
  7. KM=1.3 µM for 3-oxolitocholyl-CoA1 Publication
  8. KM=1.5 µM for 3-oxodeoxycholyl-CoA1 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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei38NAD; via amide nitrogenCombined sources1 Publication1
    Binding sitei42NADCombined sources1 Publication1
    Binding sitei92NAD; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei144SubstrateBy similarity1
    Active sitei157Proton acceptorPROSITE-ProRule annotation1
    Binding sitei161NADCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi13 – 18NADCombined sources1 Publication6
    Nucleotide bindingi190 – 195NADCombined sources1 Publication6

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

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

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:BAIA2EUBSP-MONOMER.
    UniPathwayiUPA00279.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bile acid 7-dehydroxylase 2 (EC:1.1.1.3951 Publication)
    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00000545251 – 249Bile acid 7-dehydroxylase 2Add BLAST249

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi411468.CLOSCI_03133.

    Structurei

    Secondary structure

    1249
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni3 – 6Combined sources4
    Beta strandi8 – 11Combined sources4
    Turni12 – 15Combined sources4
    Helixi17 – 28Combined sources12
    Beta strandi32 – 36Combined sources5
    Helixi40 – 53Combined sources14
    Beta strandi60 – 62Combined sources3
    Helixi69 – 83Combined sources15
    Beta strandi88 – 91Combined sources4
    Helixi101 – 103Combined sources3
    Helixi106 – 116Combined sources11
    Helixi118 – 131Combined sources14
    Turni132 – 135Combined sources4
    Beta strandi137 – 142Combined sources6
    Helixi146 – 149Combined sources4
    Helixi160 – 174Combined sources15
    Helixi176 – 178Combined sources3
    Beta strandi180 – 187Combined sources8
    Helixi193 – 196Combined sources4
    Helixi200 – 209Combined sources10
    Helixi218 – 229Combined sources12
    Helixi231 – 233Combined sources3
    Beta strandi238 – 243Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4IS2X-ray1.90A1-249[»]
    4IS3X-ray2.00A/B/C/D1-249[»]
    ProteinModelPortaliP19337.
    SMRiP19337.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CHR. Bacteria.
    ENOG410XNW1. LUCA.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 3 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    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.
    PIRiA31841.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4IS2X-ray1.90A1-249[»]
    4IS3X-ray2.00A/B/C/D1-249[»]
    ProteinModelPortaliP19337.
    SMRiP19337.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi411468.CLOSCI_03133.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4105CHR. Bacteria.
    ENOG410XNW1. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00279.
    BioCyciMetaCyc:BAIA2EUBSP-MONOMER.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 3 hits.
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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 2, 2016
    This is version 97 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

    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.