ID A4U4L4_9PROT Unreviewed; 1203 AA.
AC A4U4L4;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 13-SEP-2023, entry version 66.
DE SubName: Full=Urea amidolyase {ECO:0000313|EMBL:CAM77821.1};
GN Name=duR2 {ECO:0000313|EMBL:CAM77821.1};
GN ORFNames=MGR_3889 {ECO:0000313|EMBL:CAM77821.1};
OS Magnetospirillum gryphiswaldense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM77821.1};
RN [1] {ECO:0000313|EMBL:CAM77821.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSR-1 {ECO:0000313|EMBL:CAM77821.1};
RX PubMed=17449609; DOI=10.1128/JB.00119-07;
RA Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA Reinhardt R., Schueler D.;
RT "Comparative genome analysis of four magnetotactic bacteria reveals a
RT complex set of group-specific genes implicated in magnetosome
RT biomineralization and function.";
RL J. Bacteriol. 189:4899-4910(2007).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CU459003; CAM77821.1; -; Genomic_DNA.
DR AlphaFoldDB; A4U4L4; -.
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:0016829; F:lyase 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 Lyase {ECO:0000313|EMBL:CAM77821.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
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 1121..1199
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 770..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1203 AA; 130405 MW; C87FDFE2ECED34AE CRC64;
MFTKVLIANR GAIACRIIRT LNKMGIASVA VYSEADRHSL HVSMADEAYC IGPAPAAQSY
LRADTILDVA RRSGAQAIHP GYGFLSENPD FAEECARAGI AFIGPWPEHM RAFGLKHTAR
DLAKKAKVPL APGSGLLNDV AHAKAEAKRI GYPVMLKSTA GGGGIGLSLC RGEAELEPLF
ERVQRLARNN FKDPGLFLEK YVERGRHIEV QIFGDGKGNV VALGERDCSA QRRNQKVVEE
TPAPGISPHL RHQLCETAVK LGQAVGYANA GTVEFLYDTD ADEFHFLEVN TRLQVEHGVT
EQVTGIDLVE WMVRQAAGEP LPLADHAERA RGASIQVRLY AEDPARDFRP SSGLLTQVHW
SADARVETWV EAGLEISPYY DPMIAKIIVT GTDRADALGK MQAVLANTRI NGIETNLDYL
RALVASPAFV EGSVTTRTLE SFVHHARSVE VLAVGTQASI QDYPGRTGYW DVGVPPSGPM
DHLSMRLANH ALGNSAGTAA LELTMSGPTL KFNTDTKICL MGAEMAAALD GQPVVYGTPV
TVTAGQVLRL GTVSGAGCRA YLAVQGGFDV PDYLGSKSTF TLGKFGGHGG RALMTGDVLH
LGQPHATAQP RPVPDALMPV LGHEWEIGVL YGPHGAPDFF TDDDIEQFFA APWEVHYNSN
RTGVRLIGPK PKWARTDGGE AGLHPSNIHD NAYAIGAIDF TGDMPVILGP DGPSLGGFVC
PATIVQAELW KLGQVRPGDR VRFIRLTPAQ AALLEAKQEA EIETFAPVDT DSLAQPGGSG
PDDAVVGDIP AQGERPRVVY RRAGDKYLLV EYGPLVLDLE LRFRVHALMA ALRALAPAGI
IDMTPGIRSL QLHYDSRVLC LHELLALLMR TEESLPNNDA MEVPARIVHL PLSWDDEATQ
EAIRKYMQSV RADAPWCPSN IEFIRRINGL DSIDAVKRIV FDASYLVLGL GDVYLGAPVA
TPMDPRHRLV TTKYNPARTW TPENAVGIGG AYMCVYGMEG PGGYQFVGRT CQVWNTHKET
AEFQPGKPWL LRFFDQIRFV EVSAQELLEF RDAFPRGKAR LKIEETTFKL ADYRKFLADN
DTSIKSFKSR QQQAFDEERA RWEASGQIGY GADMPEAVDD DGDQAVPAGC VAACAPVPGS
VWKIAVQPGQ RVEAGDTLIV VESMKMEIPL LAPAAGIVAE LRCAEGRAVA LGQILAVITE
ETA
//
