ID A0A4U8Z3G2_METTU Unreviewed; 1177 AA.
AC A0A4U8Z3G2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 12.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:VFU09947.1};
GN ORFNames=MTUNDRAET4_3060 {ECO:0000313|EMBL:VFU09947.1};
OS Methylocella tundrae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=227605 {ECO:0000313|EMBL:VFU09947.1, ECO:0000313|Proteomes:UP000294360};
RN [1] {ECO:0000313|EMBL:VFU09947.1, ECO:0000313|Proteomes:UP000294360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTUNDRAET4 annotated genome {ECO:0000313|EMBL:VFU09947.1};
RA Kox A.R. M.;
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; LR536450; VFU09947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U8Z3G2; -.
DR KEGG; mtun:MTUNDRAET4_3060; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000294360; Chromosome 1.
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; 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; 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}; 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:UP000294360}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1094..1172
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1177 AA; 128529 MW; B79C0FAD2868E68D CRC64;
MFKKVLIANR GEIAGRVIRT LRKLGVRSVA VYSDADRFSP TVLAADEQVR LGPAPAAQSY
LNVEAVIAAC KATGAEAVHP GYGFLSENPG FAERLATEGI TFIGPRPEHM RSFGLKHRAR
ELAARAKAPL LPGSDLLDTL DEALSEARHI GYPVMLKSTA GGGGIGMQLC YGDEELAARL
ESVRRLGANN FGDNRVYLEK FVARARHVEV QIFGDGKGGV VALGERDCSL QRRNQKVIEE
TPAPGLSDEN RAALRAAAIS LGKAVAYESA GTVEFVYDAD QQKFYFLEVN TRLQVEHCVT
EAIFGVDLVE WMVKQAAGDF TLPSQASLVS NGAAIEARVY AEDPSKDFRP STGLLTRVKF
AEGVRVDGWI ETGVEVSPYY DPLLAKVIAY ASTREAAIEN LSRALRASDI SGLESNLPYL
AAVLDLEPFR AGEMITKTLS EFTFVPRTID VLSGGTLSSV QDWPGRLGYW NVGVPPSGPM
DDHHFRLANR IVGNLEGAAG LELTLRGPTL RFNLDTIIAL TGARMSATLD GEPASYDEPI
EVRRGQVLTL GAVNGPGNRT YLAIRNGIDA PLYLGSKATF ALGKFGGHAA GALRTGDVLR
VAETGAVSAP QKADVEPCEL THHWMIDVLY GPHGAPDFFK EDDIAELFAT DYEVHYNSAR
TGVRLIGPKP RWARADGGEA GLHPSNIHDN AYAIGAVDFT GDMPIILGPD GPSLGGFVCP
VVIIKSDLWK VGQLRPGDTI RFRPAPVRST SGALVRERGD PILHRHGEGD AAVCYRRAGD
SYLLVEFGPI VLDLGLRMRV HLLHQALIEA ALPGVIDLTP GIRSLQIHYD DAALPLRRLL
DEVMKLEANL PPVDEVEIES RIVHLPLSWN DEQAELAMRK YQELVRPDAP WCPSNIEFIR
RINGLESIED VRHIVFDASY LVMGLGDVYL GAPVATPLDP RHRLVTTKYN PARTWTPENA
VGIGGAYLCV YGMEGPGGYQ LVGRTIQMWN SWRATDAFEP GKPWLLRFFD QIRFYPVSHE
ELTDAREAFL HGRYPLKIEP TTFSLKRYKA FLRDNAKEIE AAQTRQRAAF EAERRRWEEH
GLNLFVEDRS ADDLTEIILP DGAIAIVAPM PGNVWKIEAA AGERVVAGQT LVILESMKME
IAVAAPAGGR LVEISCQAGR PVQNGQRLAV IEIEDAS
//
