ID A0A0S2HUK0_9BACT Unreviewed; 1076 AA.
AC A0A0S2HUK0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative glutamate synthase (NADPH) small subunit {ECO:0000313|EMBL:ALO13741.1};
GN ORFNames=L21SP5_00059 {ECO:0000313|EMBL:ALO13741.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO13741.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO13741.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO13741.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013118; ALO13741.1; -; Genomic_DNA.
DR RefSeq; WP_057951378.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2HUK0; -.
DR STRING; 1307839.L21SP5_00059; -.
DR KEGG; blq:L21SP5_00059; -.
DR PATRIC; fig|1307839.3.peg.57; -.
DR OrthoDB; 9796880at2; -.
DR Proteomes; UP000064893; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
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; PF01266; DAO; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893}.
FT DOMAIN 16..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 452..483
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 485..515
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1076 AA; 118776 MW; A820B6B951552CD2 CRC64;
MYKITEHPIL DIPKGKEVYF KYNGEQIKAE KGKTIAAALH QAGYPVHSHS LTNRNRSLEC
GIGKCGACEM LVDGEVRRIC ITKVDDIKEV SEIPKDYEPS KTNYPDKNPI EVHKTTVAIV
GAGPAGLAAR ATLNKHGVDN LVIDNNDTIG GQFTMQTHQF FFFEKEKKYG GMRGFDIPKE
LTMDNNEGIL LNSTVWDLLE GKRLAIKNIK TDKIYYVDAE HLIIATGAVP FMPSFENDDL
PGVYTAAVVQ KMMNNEHTLL GKNILTVGAG NIGYLTSYQA VQAGANVKAI LEAQDREGGF
PVQANRVRRL GIPIYLSHIL VKAIPNEDHT GITGAVVAEA KNFKPVPGTE RIIEGIDTIN
ICTGLVSDDA LLRKGKEVFG RNVHGAGDAI RIGEGTSAVL RGKQVAYEIM EEMSLRYNYD
DYLALSKEYI DSQQHPTKVI EEPVIPDRER MQKPFVIADC TYGFACNPCA FACPHDAITK
SSSSTVPVID FDKCVGCMQC VTLCPGLAIF GYNLKKDWLF FPVEYEVAEG EEVVLVDNDG
NKIGEGVLEK IMKKPNKTNL ARVKSSNLHG EDLVKARGFI TKANFPEQVE FAPSSNNIES
KEFICHCDDV TMDEVMKVIG DRKFISVDEI KHTTRLGMGA CRGKRCIKRL KTALAGSGIQ
IVGEATPRGP MSNQVSMGEI YPNDLHEKTI PNLNGQKIET IETKVLVAGG GIGGSALFRY
FAEAGENPIL INYERGSSWR NIAGGRPVFS VPELADIAGN NRKIFKELQE ISNIHLTDIN
YVTLAHDQAT YEALEASKAW SDAMMIEPKD FPKYIAPGFS TSNDKYMAAL VTKDCWQATP
GLVIDLIRKI GIDHGGMIHE DAKLIDLEKT DKGYIALVNT HEGKYVKYKT KHFVNALGGN
AGDFADMVGV DTGLFPVKHQ AFITRRLPYL GVNNQPLNMI IDRRNYKGFT AVYGQQLAET
GQIIGCASPA VEPLQTAKNL KINDKDFLEI VSEVFVDWLP ELSSVGFQAV WSGYYTEPRM
IIDPEKGLFV GLRGQGFMLG MYLAKMYVDA VTGKKVPEYL RRLALEGDGL QEKAFK
//
