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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//