ID A0A4R5MHF2_9BURK Unreviewed; 1210 AA.
AC A0A4R5MHF2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:TDG26547.1};
DE EC=6.3.4.6 {ECO:0000313|EMBL:TDG26547.1};
GN Name=uca {ECO:0000313|EMBL:TDG26547.1};
GN ORFNames=EYW47_01105 {ECO:0000313|EMBL:TDG26547.1};
OS Paraburkholderia silviterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2528715 {ECO:0000313|EMBL:TDG26547.1, ECO:0000313|Proteomes:UP000295722};
RN [1] {ECO:0000313|EMBL:TDG26547.1, ECO:0000313|Proteomes:UP000295722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4M-K11 {ECO:0000313|EMBL:TDG26547.1,
RC ECO:0000313|Proteomes:UP000295722};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. 4M-K11, isolated from subtropical forest soil.";
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};
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:TDG26547.1}.
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DR EMBL; SMRP01000001; TDG26547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R5MHF2; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000295722; 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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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:TDG26547.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
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 1118..1193
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1210 AA; 129249 MW; 4307656E9E2C67C5 CRC64;
MAFDKILIAN RGEIACRVIR TLKRLGIASV AVYSEADRHA MHVMLADEAV CIGPAPVAAS
YLNAEAILEA ARRTGAQAVH PGYGFLSENA AFAQACEAAG IRFIGPRPEQ MKVFGLKHTA
REVAKANGVA LLPGTGLLPD VDAALEAALS LGYPVMLKST AGGGGIGMSL CRDAAQLEAA
FASVARLGET NFANAGVYLE KFVGNARHIE VQVFGDGAGN VIALGERDCS VQRRNQKVIE
ETPAPGLTGA ERSALHATAV RLAKAVNYAS AGTVEFVFDA DTRAFYFLEV NTRLQVEHGV
TEAVTGADLV EWMIREAEGT LVPLDTLACE PHGASIQVRV YAEDPNKQFQ PSSGQLTHVA
FAPHVRVDTW VEAGTEVSAF YDPLLAKIIA TGATREAALG RLREALGGTQ LYGIETNLDY
LRAIAGSATF AAGEQTTGFL GRFAFAPHTI DVLDGGVQTT VQQTPGRLGY WDVGVPPSGP
MDDLSFRLAN ELIGNAAEAA GLEFTMVGAT LRFNTDTLFV LGGASLAATL DREPVAQWQV
VRAGAGSVLK LGGVTGAGAR ACLAVKGGLQ VPDYLGSKAT FTLGQFGGHA GRALRKGDVL
HLGPEAGHGK AGAKLDAARA PVLTHAWELA VLDGPHGAPD FLTPADIAML YEASWTVHYN
SSRTGVRLIG PKPQWARPDG GEAGLHPSNI HDNAYAIGAV DFTGDMPVIL GPDGPSLGGF
VCPVTVIADD LWKLGQLRPG DTVRFVPVPV PAPVPASVPE PAARAAHNGV RECVLYSDNR
AGDGVGVVYR RSGDRNLLIE YGPPVLDLKL RFRVHALMNW LADHRLPGII DLTPGIRSLQ
VHFDRSLLSC ERLIEHLKEA ELQLPAVDAM RVPNRIVHLP LSWDDPSTRV AIERYMQSVR
PDAPWCPSNI EFIRRINGLD SIEDVKRIVF DARYLVLGLG DVYLGAPVAT PVDPRHRLVT
TKYNPARTWT PENAVGIGGA YLCVYGMEGP GGYQFVGRTV QMWNRYRTTA EFEAGKPWLL
RFFDEIRFYE VSEAELEAWR SDFVAGRRSL RIEESVFDLG EYERFLRDEA ASIAAFKATQ
QAAFEAERER WRAAGQAGYS GESGAQEAAA AGALDEPSAL DEDCRAISAD VSGSVWKLLV
AEGERVVEGQ EVAILESMKM EVTVAASADG VIDLLDCAAG DAVVAGQRLM VIRVDAVNAN
AVSGEEAACQ
//
