ID A0A0V8J4R8_9BACI Unreviewed; 1218 AA.
AC A0A0V8J4R8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:KSU81971.1};
GN ORFNames=AS030_16950 {ECO:0000313|EMBL:KSU81971.1};
OS Fictibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU81971.1, ECO:0000313|Proteomes:UP000054099};
RN [1] {ECO:0000313|EMBL:KSU81971.1, ECO:0000313|Proteomes:UP000054099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU81971.1,
RC ECO:0000313|Proteomes:UP000054099};
RX PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA Ramana V.V., Shouche Y.S.;
RT "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL Antonie Van Leeuwenhoek 105:461-469(2014).
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:KSU81971.1}.
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DR EMBL; LNQN01000005; KSU81971.1; -; Genomic_DNA.
DR RefSeq; WP_061973796.1; NZ_KQ758619.1.
DR AlphaFoldDB; A0A0V8J4R8; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000054099; 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: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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000054099}.
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"
FT REGION 1199..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1218 AA; 133917 MW; 7CD9672A2DE81759 CRC64;
MFKKVLIANR GAIAVRIERT LRKMGISSVA VYTKADQDSL HVDLADEAVL IGEGPAKDSY
LNAELILKIA QDTGAEAIHP GYGFLSENAA FARACEEKGI AFIGPSPEQI EQFGLKHSAR
ALAEKAGVPL LPGTSLITSL EKAVAEAEKI GYPVMLKSTA GGGGIGMRVC ADNQALTDAF
DSVGRLAQTN FSNGGVFLEK YIQKARHVEV QIFGNAFGEV AALGERDCSI QRRNQKIVEE
SPAPCLAPSV REEMHGAAKR LAEDVGYRSA GTVEFLYDPK TEQFYFLEVN TRLQVEHGVT
EEVLKIDLVE WMVCEAANEL KGLHSLYDSP KGHSIQARIY AEDCQQDFRP SGGKLDGVYF
SDQARVETWI RDGLVVTPLY DPMLAKIIVH ADTRDEALDR LADALADTRF YGVTTNLQYI
GALLEDEDCR SGKVYTQMLK NFSPAEQAIE VIDGGIQTTV QDWPGRTGHW DVGVPPCGPM
DPFAFRIGNQ LLGNQDNAAG LEFTLRGGSY SFRSETVFCL TGADMQPKLD GKDIPMYRVI
KARRGQVLML GEAVKGMRSY LLVAGGLDMP LHLGSASTFT LGGFGGHGGR ALRTGDVLRL
NEGGAPSVTW LPAEKSPRLT NEWTIGVIPG PHCTEEFLQP DYLQQLTETK WEVHFNSSRT
GVRLIGPAPL WTREDGGEAG LHPSNIHDNA YAVGTLDLTG DMPILLGPDG PSLGGFVCPV
TTASAEFWKI GQLHAGDTVQ FQLLTLEEAE QLRASQEDFL VRIADPSGAA ELPGLPTIAE
RLSQNYPVLA HQEKGRIPFT IRAAGDENVL VEYGEMELDL VLRFKVHALM EAIGKRSDLP
VLDLTPGIRS LQVHIDASRM TVSLLAKEIA AINEQLPPLE EIEVPSRIVR LPLSWDDPAT
QLAIDRYQKN VRPDAPWCPS NLEFIRRVNG LNDIDDVKEI VFNANYLVLG LGDVYLGAPV
ATPVDPRHRL VTTKYNPART WTPENAVGIG GSYMCIYGME GPGGYQFVGR TVQVWNGKRD
TENFQKDRPW LLRFFDQIQF YPVSTEELTD MREEFLRGRF QVDVTETTFK LSDYLSFLES
IEESAQEFRE TQQAAFRAER ESWKAQNLAE YVSVHEAAEM TEEVLPEGAE AVRCTLPGSI
WKVLVAPGDS VRKGDVLIIE ESMKMEFPQV SPFDGTVRSV DVSPGDEVHA GQLIVSLSKE
KAGTAHENHE SSKNVIHS
//
