ID A0A2R5F6G7_9PROT Unreviewed; 1200 AA.
AC A0A2R5F6G7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:GBG13866.1};
DE EC=6.3.4.6 {ECO:0000313|EMBL:GBG13866.1};
GN Name=accC {ECO:0000313|EMBL:GBG13866.1};
GN ORFNames=NMK_1418 {ECO:0000313|EMBL:GBG13866.1};
OS Novimethylophilus kurashikiensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Novimethylophilus.
OX NCBI_TaxID=1825523 {ECO:0000313|EMBL:GBG13866.1, ECO:0000313|Proteomes:UP000245081};
RN [1] {ECO:0000313|EMBL:GBG13866.1, ECO:0000313|Proteomes:UP000245081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=La2-4 {ECO:0000313|EMBL:GBG13866.1,
RC ECO:0000313|Proteomes:UP000245081};
RX PubMed=29411502; DOI=10.1111/1462-2920.14062;
RA Lv H., Sahin N., Tani A.;
RT "Isolation and genomic characterization of Novimethylophilus kurashikiensis
RT gen. nov. sp. nov., a new lanthanide-dependent methylotrophic species of
RT Methylophilaceae.";
RL Environ. Microbiol. 20:1204-1223(2018).
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:GBG13866.1}.
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DR EMBL; BDOQ01000003; GBG13866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5F6G7; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000245081; 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:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:GBG13866.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000245081}.
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 1120..1198
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1200 AA; 131299 MW; 3AB5AA735FEBAB23 CRC64;
MFEKILVANR GEIACRIMRT LKRMGVKSVA VYSEADAGAR HVLEADEAVC IGPAPAAESY
LNAERILQVA RETGAQGTHP GYGFLSENQS FATACEAAGI AFIGPTAAQM RDFGLKHTAR
ELAEANGVPL LPGTGLLADA VEAQAEAARI GYPVMLKSTA GGGGIGMRLI WSADEFAEAF
ESVQRLSKAN FKDGGIYLEK YVQAARHIEV QIFGDGQGQV IALGERDCSV QRRNQKVIEE
TPAPNISESV RTRLAETAVR LASAIGYRSA GTVEFVYDNT SGDFYFLEVN TRLQVEHGVT
ELVSGLDLVE WMVRLAAGET LPLASYLHQP KGHAIQVRIY AEDANKNFQP SSGTLTEASF
PEDVRVDTWV VRGSEVSPFY DPLVAKVLVH AENREAAVAK MRQALAETCL AGIETNLDYL
RQVLADRVFP AGEQVTRYLN SFHYRPTTID VLEPGVQSTV QDYPGRLGYW AVGVPPSGPM
DHLAFRFANR LVGNDEGTAA LELTLIGPTL KFNCEAVIAI AGAAMQAELD GEALALWQSH
AVKAGSVLRL GRIEGAGCRA YLAVKGGFDV PEYLGSKSTF TLGQFGGHGG RTLRVGDVLH
LADAVSALPE AALLPPALMP DYTHAWEIGV LYGPHGAPDF FTDADIEMFF STDWEVHYNS
NRTGVRLIGP KPEWARADGG EAGLHPSNIH DNAYAIGTVD FTGDMPVILG PDGPSLGGFV
CPATIVQAEL WKMGQLKPGD TVRFKRLSQA EALALEEAQD RAVRTMQPET KPVFAGHAET
SPILDRIAAT ERQVGIVYRQ SGDKNLLVEY GPLVLDLNLR FRVHALMQWL EKQVIPGIID
LTPGIRSLQV HYDNRKLPVG RLLDILIQAE RELPAVEDME VPTRIVHLPL SWDDAATQLA
IEKYMQSVRK DAPWCPSNIE FIRRINGLSS VKDVKKIVFD ASYLTLGLGD VYLGAPVATP
VDPRHRLVTT KYNPARTWTP ENAVGIGGAY MCVYGMEGPG GYQFVGRTLQ MWNRWNQTAD
FRDDKPWLLR FFDQIRFYPV SAEELLQIRE DFPRGKFKLK VEEQVFSLRE YNRFLADNAE
TITAFKSTQQ AAFEAERDRW IATGQAHYSS DHDVAGAAAD TELDLPPNSR AVASHVAGNL
WQVKLQPGDR VKQGDAVVIV ESMKMEITVA APSDGTITHV FCQEGGQVAA GQDLFVIQQD
//
