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Database: UniProt
Entry: A0A0Q4C1G1_9SPHN
LinkDB: A0A0Q4C1G1_9SPHN
Original site: A0A0Q4C1G1_9SPHN 
ID   A0A0Q4C1G1_9SPHN        Unreviewed;      1198 AA.
AC   A0A0Q4C1G1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:KQM19682.1};
GN   ORFNames=ASE49_05620 {ECO:0000313|EMBL:KQM19682.1};
OS   Novosphingobium sp. Leaf2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM19682.1, ECO:0000313|Proteomes:UP000050893};
RN   [1] {ECO:0000313|EMBL:KQM19682.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19682.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM19682.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19682.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQM19682.1}.
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DR   EMBL; LMJY01000012; KQM19682.1; -; Genomic_DNA.
DR   RefSeq; WP_056770792.1; NZ_LMJY01000012.1.
DR   AlphaFoldDB; A0A0Q4C1G1; -.
DR   STRING; 1735670.ASE49_05620; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000050893; 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:UP000050893}.
FT   DOMAIN          2..445
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          121..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1117..1195
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1198 AA;  129238 MW;  E35B17B566AD6403 CRC64;
     MSFDTVLIAN RGAIATRIIR TLRRMGLRSV AVYSEADEGS NHVSEADEAI CIGGARASES
     YLNIPAILAA ARASGAGAIH PGYGFLAENV EFAQACEQAG IVFIGPTVPN IRTFGLKHSA
     RALAAAHKVP LAPGTDLLTD ENQAVFAAWE IGYPVMLKAT AGGGGIGMRV CEDEASLRES
     FEAVVRQGLS NFGDAGVFLE SYIRRARHIE VQLFGDGKGR VIALGERDCS LQRRNQKVVE
     EAPAPLLPQP VREALFDAAV RLGQAAQYRS AGTVEFLYDA DREQFFFLEM NTRLQVEHGV
     TEAVMGIDLV EWMVRGAAED FTFLDGPAPT PQGHAVQMRL YAEDPSLDYR PTSGTLTALE
     FPSDIRVETW CSSGSTVSAW YDPMLAKLIV HAPTRAEAVT AAQRAIDASR ADGIETNLRW
     LRDVVRAPAF TSGEVSTRVL DTIAYQPRSI RVISGGTATT VQDWPGRQKL WAVGVPPSGP
     MDDQSFRLGN RLLGNPEGTP GLEATVTGPS LAFVAPARIC LTGADFGATL DGVRVDPGVP
     IDVAAGQTLA MGRASSGGLR GYILFAGGLD IAPYLGSCST FELGQFGGHA ARRLLAGDTL
     HLGDGDTGAA LPQVALPAIN NEWTLRVLYG PHGAPDFFRD EDVSTFLAAA WRVHYNSNRT
     GVRLIGPKPR WARTDGGEAG LHPSNIHDNP YAIGAVDFTG DMPIILGPDG PSLGGFVCPF
     VVIAADRWKI GQLAPGDKLR FAPVTIEDAG QADAAQRALI SDGLSPAQGP VSAIETLSPI
     LAEIPEGPGR PRTVYRQQGD RNILVEYGPI VLDIELRIRV HALMTELERL ALPGIIDIVP
     GIRSLQLHFD GETMRPAAAL AALIDAEERL GDLEDFTIPS RVVHLPLSWR DPATIETIAK
     YMATVRADAP WCPDNIEFIR RINGLADADA VENLIFDANY LVMGLGDVYL GAPVATPVDP
     RHRLVTTKYN PARTWTPPNV VGIGGAYMCI YGMEGPGGYQ LFGRTIQVWN TYRQTDAFTE
     GKPWLLRFFD QIRFYPVSAE ELADWRREFP TGRRSIRIEQ SEFRLADYRA FLARNAEGIT
     AFEERRKAAF DEERAEWERR GEFDQVADLG EAEAPADAAV ELPAGSDLVE APYGGSVTKL
     LVAAGDTVTA GDKIAIIEAM KMETSVESPG SGTVAALYMQ EGQSLQPGAP MLALRRHA
//
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