ID A0A1U7IIV1_9CYAN Unreviewed; 1538 AA.
AC A0A1U7IIV1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OKH37040.1};
GN ORFNames=NIES2119_14560 {ECO:0000313|EMBL:OKH37040.1};
OS Phormidium ambiguum IAM M-71.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=454136 {ECO:0000313|EMBL:OKH37040.1, ECO:0000313|Proteomes:UP000185860};
RN [1] {ECO:0000313|EMBL:OKH37040.1, ECO:0000313|Proteomes:UP000185860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM M-71 {ECO:0000313|EMBL:OKH37040.1,
RC ECO:0000313|Proteomes:UP000185860};
RA Zhu T., Hou S., Lu X., Hess W.R.;
RT "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT Habitats.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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}.
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:OKH37040.1}.
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; MRCE01000013; OKH37040.1; -; Genomic_DNA.
DR RefSeq; WP_073594218.1; NZ_MRCE01000013.1.
DR STRING; 454136.NIES2119_14560; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000185860; Unassembled WGS sequence.
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:SF133; GLUTAMATE SYNTHASE (NADH); 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000185860}.
FT DOMAIN 22..419
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 914..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1538 AA; 168985 MW; 16E42F6D8F5E46FE CRC64;
MNSNTVPVNQ GLYDPQFEHD ACGVGFIVHQ KGQKSHEIVE QGLTILLNLD HRGACGCEAN
TGDGAGILMQ VPHKFLQKVT TAIGITLPEP GQYGVGMVYC SPDPAVRQKA QEIFAAIVAE
EGQKVLGWRD VPTDNSSLGD TAKSSEPFMC QVFIQRSANL VDDWAFERKL YVIRKRTHIA
IRASHIDPMW YPSSLSSRTI VYKGMLMPVQ VGQYYPDLQD PDMESALALV HSRFSTNTFP
SWERAHPYRY IAHNGEINTL RGNINWMHAR QSLFESELFG DDIKKIKPVI NIDGSDSLIF
DNALELMVLA GRSLPHAVMM MIPEPWTAHE SMSPEKKAFY KYHSCLMEPW DGPASIAFTD
GTMMGAVLDR NGLRPSRYYV TKDDLVIMAS EAGVLPIEPE RVALKGRLEP GRMFLVNMEE
GRIIADEEIK NTIVNQHPYA EWIKDNMVEL ANLGQGDKGT RGQGDKEILP VTSNYSLTQR
QTAFGYTFEE LRLLLTPMAR DGVEAVGAMG ADTPLAVLSD RPKILYDYFK QLFAQVTNPP
IDSIREEIIT SAETTIGAER NLLNPVPESC HLIELKSPIL SDEDLAKLKY INEGGFKSIT
LPILFDPKAG VKGLESAMEE IFQKANAAIA DGVSIIILSD RDIDKDNAPI PALLAVSGLH
HHLIREGTRT RVGLVLESGE PREVHHYATL IGYGCGAINP YLAFETIADM INEGLILNVD
YKTACKNYIK SATKGVIKVA SKIGISTIQS YRGAQIFEAI GLNKAVIDKY FTWTASRIEG
ADLEVIAQEA ILRHSHAFPD REVNGHTLDV GGEYQWRKEG EAHLFSPETI HTLQKAVRTG
NYETFKQYAK LVNEQGKKHF TLRGLLEFKE RQPVPIDEVE PIEAIMKRFK TGAMSYGSIS
KEAHESLAIA MNRIGGKSNT GEGGEDPERY TWTNEQGDSK NSAIKQVASG RFGVTSLYLS
QARELQIKMA QGAKPGEGGQ LPGRKVYPWI AKVRHSTPGV GLISPPPHHD IYSIEDLAEL
IHDLKNANRE ARVSVKLVSE VGVGTIAAGV AKAHADVVLI SGYDGGTGAS PQTSIKHAGL
PWELGLAETH QTLVLNNLRS RIAVETDGQM KTGRDVVIAA LLGAEEFGFA TAPLVTLGCI
MMRVCHLNTC PAGIATQNPQ LRQAFIGDPE HTVNFMKFIA TEVRELMAQL GFRTLSEMVG
RTDVLEPKKA VEHWKAKNID LSKILYQPEV GPEVGRYCQI PQDHGLDKSL DITVLLDLCK
SAIEKGEKVK ATLPIKNINR VVGTILGNEI TKRHWEGLPE DTVHLHFQGS AGQSFGAFVP
KGVTLELEGD ANDYLGKGLS GGKIIVYPPK GSSFVPEENI IIGNVAFYGA TGGEAYINGI
AGERFCVRNS GVNTVVEAVG DHGCEYMTGG KVVVLGKTGR NFAAGMSGGV AYILDETGDF
ATRCNTQMAD IEPLDEEDIE TIHEMIQKHR EYTGSQKAAK VLDKWEEMVS KFVKVMPRDY
KRVLECLKRA FESGLSGDEA LAAAFEENAR DVSRIGGS
//
