ID   A0A1Y5RBN5_9RHOB        Unreviewed;       464 AA.
AC   A0A1Y5RBN5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Hydrogen cyanide synthase subunit HcnB {ECO:0000313|EMBL:SLN12913.1};
DE            EC=1.4.99.5 {ECO:0000313|EMBL:SLN12913.1};
GN   Name=hcnB {ECO:0000313|EMBL:SLN12913.1};
GN   ORFNames=PEL8287_00467 {ECO:0000313|EMBL:SLN12913.1};
OS   Roseovarius litorisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN12913.1, ECO:0000313|Proteomes:UP000193827};
RN   [1] {ECO:0000313|EMBL:SLN12913.1, ECO:0000313|Proteomes:UP000193827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN12913.1,
RC   ECO:0000313|Proteomes:UP000193827};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FWFL01000001; SLN12913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5RBN5; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000193827; 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; 3.
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   InterPro; IPR041117; SoxA_A3.
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; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF17806; SO_alpha_A3; 1.
DR   PIRSF; PIRSF037495; Opine_OX_OoxA/HcnB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:SLN12913.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193827}.
FT   DOMAIN          5..312
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          372..454
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
SQ   SEQUENCE   464 AA;  48853 MW;  C0724DEAB0419926 CRC64;
     MQQIDLIIIG AGPAGMAAAQ TAADNGLSVC LLDEQPRPGG QIYRDVDRVA PLRGDILGKD
     YTEGRSLTSA LMHPQITRIP GATVWAIEEG SQVAYTANGR AAMIGAKRIL LATGALERPM
     PLPGWTLPGV MTAGAGQILL KQSGVLANSA VLAGSGPLLY LIAAQMVRAG TPPLAMVETQ
     TRHDTFSAMR HIAGALRGWR YLLKGLGMLG ELKRAGVPRY TGATDIAILG DTAATGICFT
     SGGKSHQINC DTVFLHHGVV PNTQAARSID IAHHWNNQQQ CFVPDIDHWG QTNVDTVYIA
     GDGAAIGGAK VAALAGRLSA LKIASDLDAL KADDRDRQAA PLRRAISHEL AARPFLDAAY
     PPCAQALDPS DKTLICRCEE VTAGDIRGYA KIGCLGPNQT KAFGRAGMGP CQGRYCGLSV
     TALLAKANNR SPEETGYYRI RPPLKPVTLG ELAAMQDVTK SAAE
//