ID A0A102DGV8_9SPHN Unreviewed; 1215 AA.
AC A0A102DGV8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:KUR81373.1};
GN ORFNames=AQZ50_01310 {ECO:0000313|EMBL:KUR81373.1};
OS Novosphingobium sp. Fuku2-ISO-50.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR81373.1, ECO:0000313|Proteomes:UP000056630};
RN [1] {ECO:0000313|EMBL:KUR81373.1, ECO:0000313|Proteomes:UP000056630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR81373.1,
RC ECO:0000313|Proteomes:UP000056630};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KUR81373.1}.
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DR EMBL; LLZR01000001; KUR81373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A102DGV8; -.
DR STRING; 1739114.AQZ50_01310; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000056630; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000056630}.
FT DOMAIN 7..454
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1135..1213
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1215 AA; 129803 MW; A0A434BCABD517B8 CRC64;
MTRTPLPFAK VLIANRGAIA CRIIRTLRAM GIASVAVFSE ADAGSRHVAL ADEAVPIGPA
PAGESYLNVE AILAAAKATG AEAIHPGYGF LSENTGFAEA CDRAGIVFIG PTQDNIRAFG
LKHTARDLAQ AHGVPLAPGS GLLTDAAAAA VEAARIGYPV ILKATAGGGG IGMKVCHDES
ELAEAFAMVA RLGAGNFGHG GVFLERYVAR ARHIEVQVFG DGEGHVVALG ERDCSLQRRN
QKVVEETPAP HLPAATRAAL IEAALRLTSG AKYRSAGTVE FLYDAIRDDF FFLEVNTRLQ
VEHGVTEQVT GVDLVEWMIR GAAGDFAFLD GFVAQPQGHS IQVRLYAEDP SRDFQPSSGR
LIEVAFPDGD RATLRVDGWV ESGSEVPAWY DPMLAKLIVT APSREEAIVA LQSALDATRL
AGIETNLRWL RAVVRDDVFV SGQVSTRALA DFAWQPSSIR VLTAGAATTV QDYPGRTGLW
DVGVPPSGPM DALSFRLGNR LLGNPEGAAG LEITAAGPVL QFLGAARICL TGAECGATLD
GIAVPRWTPV AVAAGQVLRV GRVQGGGLRA CLLFAGGLDA PLYLGSRSAF TLGEFGGHAG
RAVMTGDMLH LFGEATGAEA MLPAALVPAI GHEWSVRVLY GPHGAPDFFT PGDVAMICET
PWKVHYNSNR TGVRLVGPKP EWARRDGGEA GLHPSNIHDN AYAIGAVDFT GDMPIILGPD
GPSLGGFVCP FVVIQADLWK VGQLSPGDTV RFAPVSEAEA RDAERAQDAM VATLAAPAPF
TGERTPPTSP VLHTIAADGA RPTATYRRQG DRHLLVEYGP IVLDLELRLR VHALMMELDR
LALPGVIDVT PGVRSVQIHY DARLLNQGAL MDALIAAEER LGGLDDFAIP SRVVHLPLSW
QDPAIYQTID KYICAVRDDA PWCPDNIEFI RRVNGLETIE DVKRIVFDAD YLVLGLGDVY
LGAPVATPVD PRHRLVTTKY NPARTWTPPN VVGIGGAYMC VYGMEGPGGY QLFGRTIQVW
NTWVGSGKQA DAFRDGKPWL LRFFDRIRFF PVSHDELTEW RRDFPLGRRA IHIEEGLFRL
SDYRAFRETH ADSITAFETT RQAAFDEERA RWQESGEFDR VAALVEAGSG AGGDDAAIDV
PPGSELVEAP FGGSVWKLLA GEGRAVAAGE PIAVIEAMKM ECPVASPSAG VVRRVYVSEG
QVIQPGAAML AIEPA
//
