ID D6ZL54_MOBCV Unreviewed; 941 AA.
AC D6ZL54;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Putative glutamate synthase (NADPH), homotetrameric {ECO:0000313|EMBL:ADI67453.1};
GN OrderedLocusNames=HMPREF0573_11134 {ECO:0000313|EMBL:ADI67453.1};
OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS vaginalis).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI67453.1, ECO:0000313|Proteomes:UP000006742};
RN [1] {ECO:0000313|Proteomes:UP000006742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43063 / DSM 2711 / V125
RC {ECO:0000313|Proteomes:UP000006742};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001992; ADI67453.1; -; Genomic_DNA.
DR RefSeq; WP_013189157.1; NC_014246.1.
DR AlphaFoldDB; D6ZL54; -.
DR STRING; 548479.HMPREF0573_11134; -.
DR GeneID; 55565260; -.
DR KEGG; mcu:HMPREF0573_11134; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_013655_1_0_11; -.
DR Proteomes; UP000006742; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd06219; DHOD_e_trans_like1; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR42783:SF3; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006742}.
FT DOMAIN 638..736
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 554..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 103024 MW; 7176161C7DC10DE7 CRC64;
MLDTMNTVQL NILERRFNAD PKLFQAMFVA EGLAQLHAAF DTGELPEALT RKIWELLERE
DTVGRIMMRF LWNLPLGKKR VFIRAIDTWL SERYPMFAGL SDNWPAASHV APYVRPASQR
VHDFDLVTQG YLGYLTQGYT QREVDLFVWL ESMRDKHCAD RPCELGAFLQ GRKVGGCPVQ
IHVPDVMQAI AEGDFDRALR VVEESNPLPN VTGRVCPQEL QCQGVCVHKA RPIEIGQLEW
FLPQREKIVH GNEAILKRFE GRPDPWQTAE KPPIAIVGSG PSGLINAFLL ANQGFPVTVF
EAFHTLGGVL KYGIPEFRLP NELVDDVVDK IRLLGGRFVT NFVVGKTATL DDLKAAGFWR
IFVGTGAGLP KFMNVPGEHL NGVMSANEFL TRVNLMHGNL PDYDTPLPEV AGKEILVIGG
GNTAMDAART ARRLGGHVTI VYRRTKAEMP ARVEELHHAL EEGIVVAELR SPTEFHEDEN
HHVCGASVGV MELGEPDESG RRRPQPTGEI LEMDADLVIM ALGNSSNPII RDSQPDLAVQ
QWGVIKVGKD ATGGEAGSAG AGTAGGADGA DRAAETPSQA TNLEGIYSGG DASRGGSTAI
KAAGDGQAAA RQMGDLATKL EPEEVRQRVQ RAWEYTQSAA SAYRILEKRQ LSERTWEMKL
HAPAVARAVQ PGQFARFMTH EKGELIPLTV ADFDREQGWI SIVVQAVGKS TQIMCAMEVG
QAFYGIAGPL GLASKMEQFD SATQSVCFVA GGVGLAPAYP IVRKHLELGN HVTLVLGARH
RDLLFWTDPY GDPAGVSPER VEVLRRQYPD LLDVVLTSDD GSFGRQGVVT LPLEEMLRDG
RSDGRQIAEI TTIGPPIMMK FVCLLTGKYG VPTVASLNSI MVDATGMCGA CMVPFVDPET
GKLVRKHACI DGPELDGHAI DWDKFLPRFN QFKAQEKAAL R
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