ID   A0A1M6D4W9_9VIBR        Unreviewed;       475 AA.
AC   A0A1M6D4W9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Hydrogen cyanide synthase subunit HcnB {ECO:0000313|EMBL:SHI68161.1};
DE            EC=1.4.99.5 {ECO:0000313|EMBL:SHI68161.1};
GN   Name=hcnB_2 {ECO:0000313|EMBL:SHI68161.1};
GN   ORFNames=VA7868_04135 {ECO:0000313|EMBL:SHI68161.1};
OS   Vibrio aerogenes CECT 7868.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI68161.1, ECO:0000313|Proteomes:UP000184608};
RN   [1] {ECO:0000313|EMBL:SHI68161.1, ECO:0000313|Proteomes:UP000184608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI68161.1,
RC   ECO:0000313|Proteomes:UP000184608};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQXZ01000046; SHI68161.1; -; Genomic_DNA.
DR   RefSeq; WP_073605736.1; NZ_FQXZ01000046.1.
DR   AlphaFoldDB; A0A1M6D4W9; -.
DR   STRING; 1216006.VA7868_04135; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000184608; 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   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:SHI68161.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184608}.
FT   DOMAIN          5..306
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          375..426
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   REGION          430..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  51787 MW;  9B957121AC5A87BA CRC64;
     MERPRIVIIG AGPAGIRCAE TLVQQGIRPV VIDEQPQSGG QIYKRQPTPF QRSYQKLYGS
     EYKKAESVHQ TFDHLINDID YYPGTSVWAI ETQTLYAHQN ESPVEIRFDY LILCTGATDR
     VLPVEGWEQA GTYSLGGAQI ALKHQACAIG HKIAFTGTGP LLYLVAWQYL KAGATVAGVY
     DTSGFISRLK AMDKLLMKPA ALWQGLKMIG ALKRAGIPVH TGVVPRKITG EGEVSGLDII
     LKNGTCTHVD CDAVALGFHI KPETQLADLA GCEFSFDRQS ELWLPVVDSQ GRTSVPHVFC
     AGDGCRILGA DAAELSGQIV ALTVLAKIRD LNNQLEKTQS TLLARFSRMK RFGEGLLTAF
     PWPAHLIDQL SDGAVVCRCE AITKAEIKLS VREKEATEVN RSKSFSRAGM GRCQGRYCAH
     VNATIIAGER HQSPETSGRQ RSQAPVKPIP VNVYTKTPGQ SSHNHPSQKV SGKAI
//