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Database: UniProt
Entry: H1Z498_9EURY
LinkDB: H1Z498_9EURY
Original site: H1Z498_9EURY 
ID   H1Z498_9EURY            Unreviewed;       449 AA.
AC   H1Z498;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Sulfide dehydrogenase (Flavoprotein) subunit SudA {ECO:0000313|EMBL:EHQ36646.1};
DE            EC=1.8.1.- {ECO:0000313|EMBL:EHQ36646.1};
GN   ORFNames=Metlim_2605 {ECO:0000313|EMBL:EHQ36646.1};
OS   Methanoplanus limicola DSM 2279.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX   NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ36646.1, ECO:0000313|Proteomes:UP000005741};
RN   [1] {ECO:0000313|EMBL:EHQ36646.1, ECO:0000313|Proteomes:UP000005741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ36646.1,
RC   ECO:0000313|Proteomes:UP000005741};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Wirth R., Brambilla E.-M., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT   2279.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; CM001436; EHQ36646.1; -; Genomic_DNA.
DR   RefSeq; WP_004079116.1; NZ_CM001436.1.
DR   AlphaFoldDB; H1Z498; -.
DR   STRING; 937775.Metlim_2605; -.
DR   PATRIC; fig|937775.9.peg.2935; -.
DR   HOGENOM; CLU_000422_3_3_2; -.
DR   InParanoid; H1Z498; -.
DR   OrthoDB; 27922at2157; -.
DR   Proteomes; UP000005741; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EHQ36646.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005741}.
FT   DOMAIN          10..119
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          132..434
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   449 AA;  48322 MW;  388D94E2D4E76814 CRC64;
     MTKRAGDERI ADFNEVNEGI SEQNAVLEAL RCMDCVRPQC TKGCPVNIDI SAFIRAIAEE
     DFKGAAAIIK KDNMLPAICG RVCPQENQCE GLCVLGKKEK PVRIGALERF VADREREAGM
     TLPEIMSPTG KRVAVVGSGP AGITAAAELA RYGHSVTVFE SLHEAGGVLT YGIPEFRLPK
     EIVKAEIEQI LDMGVELKLN HIAGRTVSVE ELLEFDAVFL GTGAGLPSFM GIEGENLSGV
     YSANEFLTRV NLMHANAFPE YDTPVMKGSR VAVVGGGNVA MDSARVSRRM GAEVYLIYRR
     REEDLPAREE EVHNAIEEGV EFICCANPVK ILGGPAVTGI ECVRMEMCDL DESGRPCPVP
     MKGDEAVFTL DVDVVIEAIG QSPNPLLVSL IEGLERGRRG NVIVDEHGLT SVDRIYAGGD
     IATGAATVIE AMGTARKAAV SINEMLMKK
//
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