ID B2VH17_ERWT9 Unreviewed; 1205 AA.
AC B2VH17;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Urea amidolyase {ECO:0000313|EMBL:CAO95734.1};
GN Name=uahA {ECO:0000313|EMBL:CAO95734.1};
GN OrderedLocusNames=ETA_06880 {ECO:0000313|EMBL:CAO95734.1};
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO95734.1, ECO:0000313|Proteomes:UP000001726};
RN [1] {ECO:0000313|EMBL:CAO95734.1, ECO:0000313|Proteomes:UP000001726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC {ECO:0000313|Proteomes:UP000001726};
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CU468135; CAO95734.1; -; Genomic_DNA.
DR RefSeq; WP_012440436.1; NC_010694.1.
DR AlphaFoldDB; B2VH17; -.
DR STRING; 465817.ETA_06880; -.
DR KEGG; eta:ETA_06880; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_002162_2_0_6; -.
DR OMA; GGMYMCI; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000001726; Chromosome.
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:UP000001726}.
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 1122..1205
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1205 AA; 129768 MW; 4324F60DA079310F CRC64;
MFNTVLIANR GEIACRAIRT LKRMGITSVA VYSDADKNAL HVKQADIAIA LGGDKASDSY
LVIDKILNAA HRSGAQAIWP GYGFLSESLA FAAACEAAGI AFVGPSAQQI GEFGLKHRAR
ELAAAAGVPM TPGTPLLNSL DEALGAAAKI GYPVMLKSTA GGGGIGLTRC ADEAALSAAW
ESVRRLGEQF FSHAGVFLER CIDRARHVEV QIFGDGKGKV VALGERDCSL QRRNQKVVEE
TPAPNLPTAT RRALLASAVR LGERVNYRSA GTVEYIYDAA HDEFFFLEVN TRLQVEHPVT
ECVTGLDLVE CMLQVAAGEA PDWERMAQPP QGASIEVRLY AEDPLKNFQP SPGVLTDVFF
PPDIRVDSGV DGGSEVSAFY DPLIAKLIVH GEDRPSALAK MQAALGETRL HGIASNLDYL
RQVVASEAFR SGQVSTRLLD GFTPHSPVVE VLQPGTWSSI QDYPGRLGYW DIGVPPSGPM
DDYAFRLANR IVGNAEEAAG LEFTLQGPTL RFHSDALIAL TGAPCPATLD DGAVAWWQPL
AVKAGQTLTL GRMQQGCRTY LAVRNGFDVA EYLGSRSTFA LGQFGGHAGR TLRVADMLAI
SQPSLAACTT PAPVSDPQPL PVAAQPVYGD EWRIGVLYGP HGAPDFFTQR SIDNFFAAEW
QVHYNSNRLG VRLVGPKPGW ARLNGGEAGL HPSNVHDCEY AIGAVNFTGD FPVILTRDGP
SLGGFVCPVT IAKAELWKVG QVKPGDRIRF HPIGVEEASA LEQSIAHAVA TLKPGHAPAF
AVPSLAAGAN GSASVLASIK ASATTPTAIY RQAGDNYILL EYGDNVLDLA LRLRVHLLMT
ALNEVGQPGV EELSPGVRSL QIRYDSRIIS QKKLMALLLE LESDLGEVSQ MQIPSRIVHL
PLAFEDSATL GAVERYRQTV CASAPWLPNN VDFIQRINGL SSRDAVSRTL FDASYLILGL
GDVYLGAPCA VPIDPRHRLL SSKYNPARTF TAEGTVGIGG MYMCIYGMDS PGGYQLVGRT
LPIWNKFLKN AQFAAGEPWL LRFFDQVRFY PVSEAELEVL RDDFREGRAS IRIEQSVFDF
AEHTQFLHDN AQSIAEFRQK QASAFEAEVA LWAQEEEATP PAAEEMLPAP PEEESGCLVS
ADLNGNIWKV LVQPGDEVAA GQPLIIVEAM KMELAIAAPQ AGCVKRIACQ PGRPIAPGDA
LLWLE
//