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Database: UniProt
Entry: U7DBV6_9BACT
LinkDB: U7DBV6_9BACT
Original site: U7DBV6_9BACT 
ID   U7DBV6_9BACT            Unreviewed;       277 AA.
AC   U7DBV6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Glutamate synthase, small subunit {ECO:0000313|EMBL:ERP31890.1};
GN   ORFNames=CALK_1105 {ECO:0000313|EMBL:ERP31890.1};
OS   Chitinivibrio alkaliphilus ACht1.
OC   Bacteria; Fibrobacterota; Chitinivibrionia; Chitinivibrionales;
OC   Chitinivibrionaceae; Chitinivibrio.
OX   NCBI_TaxID=1313304 {ECO:0000313|EMBL:ERP31890.1, ECO:0000313|Proteomes:UP000017148};
RN   [1] {ECO:0000313|EMBL:ERP31890.1, ECO:0000313|Proteomes:UP000017148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACht1 {ECO:0000313|EMBL:ERP31890.1,
RC   ECO:0000313|Proteomes:UP000017148};
RX   PubMed=24112708;
RA   Sorokin D.Y., Gumerov V.M., Rakitin A.L., Beletsky A.V., Damste J.S.,
RA   Muyzer G., Mardanov A.V., Ravin N.V.;
RT   "Genome analysis of Chitinivibrio alkaliphilus gen. nov., sp. nov., a novel
RT   extremely haloalkaliphilic anaerobic chitinolytic bacterium from the
RT   candidate phylum Termite Group 3.";
RL   Environ. Microbiol. 0:0-0(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR006816-1};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR006816-2};
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:ERP31890.1}.
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DR   EMBL; ASJR01000008; ERP31890.1; -; Genomic_DNA.
DR   RefSeq; WP_022636591.1; NZ_ASJR01000008.1.
DR   AlphaFoldDB; U7DBV6; -.
DR   STRING; 1313304.CALK_1105; -.
DR   PATRIC; fig|1313304.3.peg.1060; -.
DR   eggNOG; COG0543; Bacteria.
DR   OrthoDB; 9778346at2; -.
DR   Proteomes; UP000017148; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd06219; DHOD_e_trans_like1; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR   PANTHER; PTHR43513:SF3; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT-RELATED; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW   FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017148}.
FT   DOMAIN          1..95
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         62..64
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT   BINDING         222
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         225
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         237
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   277 AA;  29863 MW;  895BABDC3EC4C789 CRC64;
     MAEILQISNL SEHIYRVRLV APRIAKRRKA GQFVIVRVTP DGERIPLTIA NASAEEGWIE
     LIIQAVGEST RVLRDMQVGD HLEDLAGPLG RATKVEKVGR VLCIGGGVGI APLRPIAEAF
     KAAGNHVTTI LGARTSDLII LRDDMDQISD ELYIATDDGS AGEKGFPTDI FARLLDTGNT
     YDEAVVVGPP VMMKFTSLKT LDAGVPTMCS LNPIMIDGTG MCGGCRVTVA GEPRFACVDG
     PEFDAASVEW DDLLNRLSGY DKIAERNHTC RIGTDEK
//
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