ID K8E0F6_9FIRM Unreviewed; 484 AA.
AC K8E0F6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Sulfide dehydrogenase (Flavoprotein) subunit SudA {ECO:0000313|EMBL:CCO08920.1};
DE EC=1.8.1.- {ECO:0000313|EMBL:CCO08920.1};
GN ORFNames=DESHY_60092 {ECO:0000313|EMBL:CCO08920.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO08920.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO08920.1, ECO:0000313|Proteomes:UP000009315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCO08920.1}.
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DR EMBL; CAOS01000013; CCO08920.1; -; Genomic_DNA.
DR AlphaFoldDB; K8E0F6; -.
DR STRING; 1121428.DESHY_60092; -.
DR eggNOG; COG0493; Bacteria.
DR Proteomes; UP000009315; Unassembled WGS sequence.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:RHEA.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR006004; SudA-like.
DR NCBIfam; TIGR01316; gltA; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCO08920.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009315}.
FT DOMAIN 36..146
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 157..465
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 484 AA; 52136 MW; 1E724B6C661475BF CRC64;
MPLTGPVAAV AEEVNAMAKQ IIPQKHAMPQ QDPLVRSKNF AEVALGYDEE LAVAEAERCL
NCKKPLCKQG CPVGVDIPEF IALVKERKFA EAARVIKRTN ALPAVCGRVC PQEHQCEKYC
VVGKKHEPVA IGRLERFVGD YVMNMETEIE KAAPTGYQVA IVGSGPAGLA CAADLARWGH
SVTVFEALHT PGGVLMYGIP EFRLPKRIVQ LEIENLKKMG VKIETNAVIG QIASLDELLN
EEGFDAVFLG TGAGTPYFMN LPGENLNGVY SANEFLTRAN LMKAYRFPQS ATPIKVGKKV
AVLGGGNVAM DAARTALRLG AEEVYIVYRR SRAELPARLE EIEHAEEEGV KFLFLTNPTR
YIGNQEGWLT GLTCIKMELG EPDASGRRKP VPVDGSEFLL PVDVAIVAIG QGPNPLITKT
TPDLATNRRG NILADETGKT SKEGVYAGGD VVTGAATVIK AMGAGRAAAR SIHDYLMSKG
PQKN
//
