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Database: UniProt
Entry: A0A2R8ASU7_9RHOB
LinkDB: A0A2R8ASU7_9RHOB
Original site: A0A2R8ASU7_9RHOB 
ID   A0A2R8ASU7_9RHOB        Unreviewed;       464 AA.
AC   A0A2R8ASU7;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Hydrogen cyanide synthase subunit HcnB {ECO:0000313|EMBL:SPF79122.1};
DE            EC=1.4.99.5 {ECO:0000313|EMBL:SPF79122.1};
GN   Name=hcnB {ECO:0000313|EMBL:SPF79122.1};
GN   ORFNames=ALP8811_03057 {ECO:0000313|EMBL:SPF79122.1};
OS   Aliiroseovarius pelagivivens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Aliiroseovarius.
OX   NCBI_TaxID=1639690 {ECO:0000313|EMBL:SPF79122.1, ECO:0000313|Proteomes:UP000244911};
RN   [1] {ECO:0000313|EMBL:SPF79122.1, ECO:0000313|Proteomes:UP000244911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8811 {ECO:0000313|EMBL:SPF79122.1,
RC   ECO:0000313|Proteomes:UP000244911};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OMOI01000002; SPF79122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8ASU7; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000244911; Unassembled WGS sequence.
DR   GO; GO:0050622; F:glycine dehydrogenase (cyanide-forming) activity; IEA:UniProtKB-EC.
DR   CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR017224; Opine_Oxase_asu/HCN_bsu.
DR   PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF037495; Opine_OX_OoxA/HcnB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:SPF79122.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244911}.
FT   DOMAIN          5..300
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          372..423
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   464 AA;  49909 MW;  9F483B268A26C3A5 CRC64;
     MNARQCVIIG AGPAGMSAAM TLIAHGVTPL VLDRGAQAGG QIYRSAANSL LPDTTVLGPE
     YAKGADLVAA YQNSPADHVA GADVWHIGVD GKILFSKDAA THQVGAREML LCPGAIERPM
     PIKGWTLPGV MTAGAAQVML KSDAMVAEGA VFAGSGPLLY LIVAQYLRLG VKVAALVDTT
     PHQNYLKAAP FLPGALREPK MLQKGLSLLW EIRRAGVAVH RNVTELEVIG ETRAEGLRIN
     GRQVIPAETV FLHHGVMPNP NMTRALRLTH AWNEDQLTWH VARNRFGQSS LSHAAVAGDG
     AGIVGADGAE AEGRLAALNM LCRLGRISVE ERDRKASGDH ATLHRLAAVR RFIDRLYRPL
     DHLRVPQDED TLVCRCEERS LGDLRAGFAA GATDPNALKS LTRCGMGPCQ GRQCGPMVSQ
     LLSTWREDPI ADVGYYRLRS PQRLLSLKEL SRFHKLGQAQ EAAE
//
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