ID F6AAW7_PSEF1 Unreviewed; 1224 AA.
AC F6AAW7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:AEF23236.1};
DE EC=6.3.4.6 {ECO:0000313|EMBL:AEF23236.1};
GN OrderedLocusNames=Psefu_3274 {ECO:0000313|EMBL:AEF23236.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF23236.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF23236.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) 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; CP002727; AEF23236.1; -; Genomic_DNA.
DR RefSeq; WP_013792363.1; NC_015556.1.
DR AlphaFoldDB; F6AAW7; -.
DR STRING; 743720.Psefu_3274; -.
DR KEGG; pfv:Psefu_3274; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR HOGENOM; CLU_002162_3_0_6; -.
DR OMA; TLQMWNR; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000000686; Chromosome.
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:AEF23236.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000000686}.
FT DOMAIN 1..450
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 1142..1222
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1224 AA; 132556 MW; 41FBDD0034512389 CRC64;
MFEKLLIANR GAIACRILRT LRELDVKGVT VYSEADVASL HVQQADEAFS LGEGPAAQTY
LVVDKILAVA RQTGAKAIHP GYGFLSENAA FAEACEAAGI AFVGPTPEQL RVFGLKHTAR
ALAKQHGVPM LEGTELLENI DAALVAGEQV GYPVMLKSTA GGGGIGMRVC RSAAELSDAF
DAVKRLGQNN FSDSGVFIEK YIQRARHLEV QVFGDGQGEV LALGVRDCSV QRRNQKVLEE
TPAPNLPAGM NEALCAAAIK LAKAVNYRSA GTVEFVYDSE AERFYFLEVN TRLQVEHGVT
EQVWGVDLVR WMIELAAGDL PPLGELGKAL KPSGHAIQAR LYAEDPGRDF QPSPGLLTAV
QFPEADGKTL RIDTWVEAGC EIPPYFDPMI AKLITWQPSR EQASAALDKA LADSVLYGVE
CNRDYLRQIL SDAPFASGSP WTRCLENLTY QATTFEVLSA GTQTTVQDFP GRIGYWAVGV
PPSGPMDSRA LRLGNRLLGN DEGAAALEIT MSGPLLRFNT DAVIAVTGAE IPLGIDGVEQ
PMNTALLIAA GSTLALGTIA GAGARSYLSV RGGIQVPDYL GSKSTFTLGQ FGGHGGRALR
AGDVLHIPSL ADRQAGNQLP AELYPALPAV REIRVIYGPH GAPEYFTPAY IDTFFATAWE
VHFNSSRTGV RLIGPKPEWV RESGGEAGLH PSNIHDNPYA IGAVDFTGDM PVILGPDGPS
LGGFVCPVTI IEADLWQLGQ LKAGDKVRFI AVDIATAREL AKTNARECTS LCGSGRAAFR
FSRDAGDTPI ADKSALTKAT VPTKASELQS PIVLDIGQDD TRLVARLSGD THLLLEIGQP
ELDLVLRFRG HALMQALEAK QIDGVIDLTP GIRSLQVHYQ PETLALQKLL AIVAGEWDAV
CAAKDLKVPS RIVHLPLSWD DPACQLAIEK YMTTVRKDAP WCPSNLEFIR RINDLPNLDE
VYRTVFDASY LVMGLGDVYL GAPVATPLDP RHRLVTTKYN PARTWTAENS VGIGGAYMCV
YGMEGPGGYQ FVGRTLQMWN RYREVAAFGG KPWLLRFFDQ IRFYPVSADE LLRIRRDFPL
GRFELRIEES ELALADYQQF LTDEADGITA FRDQQRTAFA AERQRWIDSG QAHFESDEGV
AEVTEDAPLD AGQHSVDSHI AGNLWQVQVE AGARVEAGDV LVILESMKME IPITAPVAGI
VREVRVQPGA AVRVGQRVAV IEQA
//