ID Q1GC81_RUEST Unreviewed; 454 AA.
AC Q1GC81;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Formiminoglutamate deiminase {ECO:0000313|EMBL:ABF65735.1};
GN OrderedLocusNames=TM1040_3003 {ECO:0000313|EMBL:ABF65735.1};
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF65735.1, ECO:0000313|Proteomes:UP000000636};
RN [1] {ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABF65735.1, ECO:0000313|Proteomes:UP000000636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040 {ECO:0000313|EMBL:ABF65735.1,
RC ECO:0000313|Proteomes:UP000000636};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP000377; ABF65735.1; -; Genomic_DNA.
DR RefSeq; WP_011540313.1; NC_008044.1.
DR AlphaFoldDB; Q1GC81; -.
DR STRING; 292414.TM1040_3003; -.
DR KEGG; sit:TM1040_3003; -.
DR eggNOG; COG0402; Bacteria.
DR HOGENOM; CLU_012358_3_0_5; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000000636; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR010252; HutF.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR02022; hutF; 1.
DR PANTHER; PTHR11271:SF48; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11271; GUANINE DEAMINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000636}.
FT DOMAIN 46..425
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 454 AA; 49320 MW; D8B5F83D8EE58407 CRC64;
MQTIFAATAC LPEGWAKDVR LTIKDGQISR IETGSAPVPG DTRVDVLLPA LANLHSHSFQ
RAMAGRTEFR GAGQDSFWTW RELMYRFLDH LTPDQYEAIA ALTFMEMMEA GYASVGEFHY
VHHQPGGTAY QSLSELSQRV MAGAQQTGIG LTHLPVLYTY GGAQQQPLTG GQMRFGNDVE
RFSRLVTEAR DAAQELGRDT RVGIAPHSLR ATSPEDLAAV LPLAADSPIH IHIAEQPREV
AEIKVWLGAR PVEWLLGNAP VDNQWCLIHA THMTETETRH MAHSGAVAGL CPITEANLGD
GPFNGAHYLR EGGRFGVGSD SNVRISLVEE LRTLEYSQRL RDLARNVLVP AEGSVGETLY
LGAARGGAQA LGRDAGRLEI GALADLVAID CARPALFGLP EHQILDGLCF AADDHSVTDV
WAAGRHMVQT GRHIARDSIL ASYRKAITSL LAEL
//
