ID   A0A378YPY9_9NOCA        Unreviewed;       991 AA.
AC   A0A378YPY9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=sn-glycerol-3-phosphate dehydrogenase subunit C {ECO:0000313|EMBL:SUA78823.1};
GN   ORFNames=NCTC1934_03529 {ECO:0000313|EMBL:SUA78823.1};
OS   Nocardia otitidiscaviarum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1823 {ECO:0000313|EMBL:SUA78823.1, ECO:0000313|Proteomes:UP000255467};
RN   [1] {ECO:0000313|EMBL:SUA78823.1, ECO:0000313|Proteomes:UP000255467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC1934 {ECO:0000313|EMBL:SUA78823.1,
RC   ECO:0000313|Proteomes:UP000255467};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; UGRY01000002; SUA78823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A378YPY9; -.
DR   STRING; 1406858.GCA_000710895_05345; -.
DR   Proteomes; UP000255467; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255467}.
FT   DOMAIN          55..283
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  109086 MW;  A4312E8D69465CB2 CRC64;
     MTRMDDSGVE RADDRSESPR IDTRTLEREL RMAVRGEVRF DSGTRATYAT DASNYRQVPL
     GVVLPRTPED AEAAVAVCRA HDAPVLSRGG GTSLAGQCCN SGVVLDWSKF CDRVVSVDRD
     ARTAIVEPGI ALDELNDRLA DTGLMVGPRP STHDSCTIGG MIGNNSCGST AQEYGKMADS
     VRRLEVLTYA GTRAWVGAAA DDAQAALIER GGELGEIVRR LRDLRDRYAD EIRSRFPDIP
     RRVSGYNLDA LLPERDFHLA RLLVGSESTL VTVLRAEIEL VPRPGAVTLA VLGYPDIATA
     ADAVPRILPY EPSALEAIDH RLVELERTRA LATAAARQLP EGRGWLMVQF HGEDQEAADR
     KAHTMMREVC DRTGATGVLL DDPRRQAEVW AAREAGLGAT AYPPDGPETH EGWEDAAVPP
     DRLGDYLRDF EKLLDEFGYQ SASLYGHFGH GCVHTRIPFD LRTADGIARY RRFVARAARL
     VTEYGGSLSG EHGDGQSRGE LLPIMFGDRV VRAFTELKDI FDPRDRMNPG KVARPHRLDQ
     NLRQGVDYRP WEPETHFAFP HDDHRFSVAA GRCVGVGKCR GHQGGVMCPS YRVTREEEHS
     TRGRARLLFE MLNGDVITDG WRSEEVHDAL DLCLACKGCR SDCPVDVDMA TYKAEFLSHY
     HHNRIRPMAH YSMGWIPLWA RLATSMSGFA NAVVQSRTLG QLVKRAGGMA PARAMPRFAD
     TRFTTIFPEL HQDSTGTRGT VLLWPDTFTN NFEPEVARAA VRVLNAAGFT VRVPTRAVCC
     GLTWISTGQL PTAKRILRRT LRTLRPELRL STPVVVLEPS CAAVFRSDLP ELLHGDEDAH
     RLAEQTRTLA ELLAERAPEW QPPRLDSHAV VQPHCHHHAI LGFDPDRDLL SRTGLDADVL
     DAGCCGLAGS FGFERGHYDV SVACAEDKLM PAIRAQPPGT LITADGFSCR TQIRELAPDT
     APVHSAQLLA RGLDRSSTAH APDRDTGPVV P
//