ID   Q488K4_COLP3            Unreviewed;      1535 AA.
AC   Q488K4;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Putative glutamate synthase, ferredoxin-dependent {ECO:0000313|EMBL:AAZ27989.1};
GN   OrderedLocusNames=CPS_0761 {ECO:0000313|EMBL:AAZ27989.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ27989.1, ECO:0000313|Proteomes:UP000000547};
RN   [1] {ECO:0000313|EMBL:AAZ27989.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H {ECO:0000313|EMBL:AAZ27989.1};
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716}.
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DR   EMBL; CP000083; AAZ27989.1; -; Genomic_DNA.
DR   RefSeq; WP_011041610.1; NC_003910.7.
DR   STRING; 167879.CPS_0761; -.
DR   MEROPS; C44.003; -.
DR   KEGG; cps:CPS_0761; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_6; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00982; gltB_C; 1.
DR   CDD; cd00713; GltS; 1.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR002489; Glu_synth_asu_C.
DR   InterPro; IPR036485; Glu_synth_asu_C_sf.
DR   InterPro; IPR006982; Glu_synth_centr_N.
DR   InterPro; IPR002932; Glu_synthdom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11938:SF145; GLUTAMATE SYNTHASE, LARGE SUBUNIT; 1.
DR   Pfam; PF00310; GATase_2; 1.
DR   Pfam; PF04898; Glu_syn_central; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   Pfam; PF01493; GXGXG; 1.
DR   SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
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}.
FT   DOMAIN          21..420
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1535 AA;  168285 MW;  CF004F7C87A4EA5F CRC64;
     MNDMSKKSQG LYRAEFEHDS CGIGFVANLK GKKTHDIIEN ALTMLSCMEH RGGTGFDVKS
     GDGAGILIQI PHDFLSQETE KLGFSLPDAG NYGVGMIFFP RDKAQSEACR EILNQNITEL
     GLTLLGYRDV PGDNSMLGAA SFDSEPNIEQ VFIAKPAALT AQEFERKLFV LRKYTSHKIN
     ASGITERDEF YVTSMSSTKI VYKGQFTTQQ VRQYYLDLQD ERTISGMAMF HSRFSTNTFP
     AWRRAQPFRY IAHNGEINTV RGNINWMNAR EALFSSVNFS DAELKMLNPI CNNDNSDSAN
     LDMAIELLVL SGRSLAQVMM MMVPEAWQTQ TDMDATKHAF YEYYACIMEP WDGPASLSFS
     DGNVIGATLD RNGLRPSRYL LTEDGTLVMG SETGTLCVDQ STVVEKGRLQ PGKIFIADLK
     QGRIISDDEV KAQVSSAQPY GKWLADNKVE LDKLPVPIAS IAQPPLAELR KMQKAFGYTS
     EDLNLVLAGM VGTSKEPLGA MGTDTPLAVL SSRPQQLSHY FKQLFAQVTN PPIDPIREEL
     VMSLRGYIGK SFNLLDETPE HCHKVEIEQP VLTIDQLRKL QYIDNNHLQS KTIAITFKAS
     GEAGALKKAL DRVCFNAKSA VEDGYEILIL SDREVDSDHV AIPSVLATAA VHHYLIREKL
     RSGADIILES GDIRETHHFA TVIGYGAAAV NPYLALESMY GLRDEGVLDS KLTDEEIVAK
     YTAAVGSGLL KTFSKMGIST LQSYLGAQVF EALGINSDVI DEYFTGTVSR IQGLSLDQIA
     QEALLRHREG FPEASRIAVE NLLPTGGEYS WRNDGERHLF SPTVIRLLQH STASNDTNQF
     KQYAKTVDDQ SKEAFTLRGL LELNSDRPSI PLSEVEPIEN IFKRFASGAM SFGSISWEAH
     TTLAIAMNRI GGKSNSGEGG EDPIRYTPLE NGDSMNSRIK QVASGRFGVT SHYLTNADEL
     QIKMAQGAKP GEGGQLPGDK VDAWIGKTRG STPGVGLISP PPHHDIYSIE DLSQLIFDLK
     NANREARVNV KLVSEAGVGT IASGVAKAYA DVVLIAGHDG GTGASPLSSI KHTGLPWELG
     LAETHQTLVR NHLRSRITVQ TDGQLKTPRD LAIATLLGAE EYGMATTALV VEGCIMMRKC
     HLNTCPVGIA TQDKGLRDKF TGRADILVNF FTMMAEGLRE IMAELGFKTI EEMVGQTQCL
     KQLENVDHWK YQGLDLTPLL HKEESHESET LYQSINQKHL IDDIIDRKMI KDAQVALDSQ
     QSVSLEYDVI NTDRTIGAMI SNEISKKYQA EGLPENTIKV KFNGSAGQSF GCFSAKGLHF
     ELEGDANDYF GKGLSGANLV VYPSKQAKFI ASENILIGNV AFFGATSGSA FIRGIAGERF
     CVRNSGATAV VEGVGDHGCE YMTGGKAVIL GATGRNFAAG MSGGVAYVLD DNKDFAPKCN
     MEMVSLETVD TDAESLELKA LIAEHFAATG SDVANELLND WDNNVKRFVK VMPVDYKRMQ
     GYMNDVRESG KFESEYDIAV QAFDIHLNKL ASAKA
//