ID A0A0F6TBE9_9CORY Unreviewed; 1527 AA.
AC A0A0F6TBE9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glutamate synthase family protein {ECO:0000313|EMBL:AKE39124.1};
DE EC=1.4.1.14 {ECO:0000313|EMBL:AKE39124.1};
GN Name=gltB {ECO:0000313|EMBL:AKE39124.1};
GN ORFNames=UL81_05795 {ECO:0000313|EMBL:AKE39124.1};
OS Corynebacterium camporealensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39124.1, ECO:0000313|Proteomes:UP000033566};
RN [1] {ECO:0000313|EMBL:AKE39124.1, ECO:0000313|Proteomes:UP000033566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39124.1,
RC ECO:0000313|Proteomes:UP000033566};
RX PubMed=26021938;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL Genome Announc. 3:e00572-15(2015).
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}.
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DR EMBL; CP011311; AKE39124.1; -; Genomic_DNA.
DR KEGG; ccj:UL81_05795; -.
DR PATRIC; fig|161896.4.peg.1136; -.
DR HOGENOM; CLU_000422_8_2_11; -.
DR Proteomes; UP000033566; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
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; 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 ECO:0000313|EMBL:AKE39124.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033566}.
FT DOMAIN 18..412
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1527 AA; 166757 MW; 89B5F9847E265EC3 CRC64;
MAVKAQGLYS PDYEHDACGV AFVADMHGRA SRDIVDKGIQ ALINLDHRGA AGAEPNTGDG
AGILIQIPDA FCRAVAAENG FDLPEAGAYA TGIAFLPRMR MAMLDAKREI EAIAEEEGAK
VLGWREVPVD PSDLGEMSKG AMPTFQQIFL SAEGKTGIDL DRVMFFVRKR CERELGTKNG
EDTIYFPSLS SRTMIYKGML TTPQLGNFYA DLQDPRLESA LAIVHSRFST NTFPSWPLAH
PFRMVAHNGE INTVKGNENW MRAREALIES ELLGPLDRVL PVCDSSGSDT ALFDEALELL
HLGGRSLPHA VMMMIPQAWE HQDNIDPDLR DFYEYHSCLM EPWDGPAAVA FTDGTLIGAV
LDRNGLRPGR IWITEDGLVV MASETGVLDI EPSKIVKRTR VQPGRMFLVD TEHGRIVEDD
EIKQRLAHAQ PYGEWIRDNF VHIEDLPQTE YKYMPHNRAV LRQRTFGITE EDVDLIIRPM
ALTGAEAIGS MGSDTPIAAL SARPRMIYDF FAQRFAQVTN PPLDSIREKN ITSMFTLMGA
QSDVLNPDAA AARRLHLDGP VIDNHQLATL IHANDEGKAE HFGAAVISGL YPVAHHGRGL
REAIDRVRRE VSAAIAEGKT LIVLSDRESD ERFAPIPSLL LTSAVHQHLV AERTRTRASL
VIESGDAREV HHLAMLISFG ADAINPYMAF ETIDELRMKG QLGELTLDEA CGNYISAATT
GILKVMSKMG IAAVSSYRGA QLADCTGLHQ DLLEDYFGGI SSPISGMGLE DIAADVEARH
RSAFLPRPEE NAHRDLELGG EYKWRREGEF HLFNPETIFK LQHATKTGQY KIFKDYTRAV
DDQSKRLATI RGMFEFVPDR EPISIDEVES VADIVKRFST GAMSYGSISA EAHEVLAIAM
NRLGGMSNSG EGGEDPKRFE VESNGDWKRS AIKQVASGRF GVTSHYLNNC TDIQIKMAQG
AKPGEGGQLP PHKVYPWVAE VRITTPGVGL ISPPPHHDIY SIEDLAQLIH DLKSANPDAR
IHVKLVAERG IGAVAAGVSK AHADVVLVSG HDGGTGASPL TSLKHAGGPW ELGLAETQQT
LLLNGLRDRI RVQADGQLKT GRDVIIAALL GAEEYGFATA PLVVEGCIMM RVCHLDTCPV
GIATQNPELR KKFTGRADHV VNFFTFIAEE VREYLAQLGF RSLDEAIGQA QVLRQNKEVG
HDRAQNLDLS PIFERIESPH FRNQNLRCTK TQNHSLDEAL DNQIITASQL TIDAAAAKNS
ANAPSWMTGG EDPSISLEYP ISNVDRSVGT MLGSRLTRAA GVNGLPSDTL NLTFRGSAGN
SFGAFVPRGI TMNLVGDAND FVGKGLSGGR IVVRPDDNEP EQLEHNPDII AGNVTAYGAT
SGELFIRGTV GERFCVRNSG ATAVVEGVGN HGCEYMTGGK VVILGEIGEN FGAGMSGGIA
YIQNSPELES RLNKDVANGI EELDDDDIEF LSKTIAEHIT RTGSKTKARP TDMVKIVPAP
YRRVLDVIEE ARKDNRDENE AIMEAVK
//
