ID S3VJ58_9LEPT Unreviewed; 1979 AA.
AC S3VJ58;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Carbamoyl-phosphate synthase L chain, ATP-binding domain protein {ECO:0000313|EMBL:EPG76490.1};
GN ORFNames=LEP1GSC058_1371 {ECO:0000313|EMBL:EPG76490.1};
OS Leptospira fainei serovar Hurstbridge str. BUT 6.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193011 {ECO:0000313|EMBL:EPG76490.1, ECO:0000313|Proteomes:UP000014540};
RN [1] {ECO:0000313|EMBL:EPG76490.1, ECO:0000313|Proteomes:UP000014540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUT 6 {ECO:0000313|EMBL:EPG76490.1,
RC ECO:0000313|Proteomes:UP000014540};
RA Harkins D.M., Durkin A.S., Selengut J.D., Sanka R., DePew J., Purushe J.,
RA Ahmed A., van der Linden H., Goris M.G.A., Hartskeerl R.A., Vinetz J.M.,
RA Sutton G.G., Nelson W.C., Fouts D.E.;
RL Submitted (APR-2013) 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:EPG76490.1}.
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DR EMBL; AKWZ02000001; EPG76490.1; -; Genomic_DNA.
DR RefSeq; WP_016547759.1; NZ_AKWZ02000001.1.
DR STRING; 1193011.LEP1GSC058_1371; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000014540; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
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; PF01039; Carboxyl_trans; 3.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 3.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding 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; PS50989; COA_CT_CTER; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 45..496
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 167..362
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1708..1968
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1979 AA; 222238 MW; F31422C0DA1C37F4 CRC64;
MKSEEKINID NTHDFSDIES FRSLLRTKNK SLSDTVRNRR EREGRLQKVL IANRGEIAKR
FFLALHEEGI RSVAVVADQD RGQSWFEFAD EVIYIGEAKN YANIPAICAA VLESGANAVY
PGYGFLSENY HFVDRLCEIE KFYGHEIIFM GPKASVMRSV GNKLDARNLA IQNGIPLFQG
SGSITGLKEA ESEAERIGFP VILKLDAGGG GKGMIVIRSI EELPPAIESA VRIGRNSYGN
DTFYLEKYIE HPAHFEVQIF NGVAVGIRKC AVQRRNQKII EESGESFLPP NTQLQLLSSA
EKLASISGYS ERCGAGTVEF LLDRQTGQFG FLEMNTRLQV EYAVTDQSLG IDLAKWQIFL
FDEREQKIPY HSVLRMRFRE RDHSIQCRIY AEDPYQNYSP SPGKIRELEL PTFNGIRCDF
GFKKGDVIPG DFDPMIGKLV SFGKDRPEAL LRMERALSEL YLSGITSNIE QLLSIVRHHR
FIEGDYDNRL LEEYPELTAT DHSLFEDSVT FACISETLRC NGESVSDVFR KRDLTKILYS
QDLDESPYRY KVWIDETSYH IFLLRVGLRE FLVGGDSLPA RKIQVSRSSS DGKQFLAESN
GRSVSVRIDA KPNFHLIRFS GSSGKLHYSR LRITSEGQKE SGDEQGVLRS PFQGTFVKLF
EDPISKKNWA EGSVIKRGDP LLVISAMKME TVLKSPADGI VSYLIENGNL SKLIRGATAA
GQILGKSFSE GEVLAKITSE ILTKEIISGN STIADRTIST DRSLIEQWNK IPEATEDQLS
LAFTQNLDIG KQRKEILRIL YSVILGFSGG SETEAKITNL FSAMDVTKIA KERKEADEWA
ALLTFLLKYV VLIRRLFSSD FGSSHSHFGE LQRSLLNWDT EGFKPYKGTS RLLSRAFSFY
EVKPWVSFRR LREQGEAFYF ILIAYKNLMN YSKLYADILE KLSFLLPASK IVNLHLHELL
ALEERERDPM FEAVVRRILS VRKASDFNAP EGVRTLSKRH ISKYIQFMKD PWALASNSSA
KKDRLLLSFS ETLPLIPENI PEKIRSTIDS KLEYWKSQGK ISRLDSLIEN KFLYSFEVKN
KIEYVLFVFI PVTSLRREWN DLDQAFHFPE LEDQAISGAA LLQSLNALRS ASSFRLELIA
MESEAPSSER RIDSSLDYET LNQTASSMME FFLHGAFSSL TLEIGDGKGI PSKRYSFFFR
DGKLRIDSLG KDDFRFPYAE VCDPKDRKLY EKGKWPLERW VEESFDPDSF EEVLVPNLDF
GETENSDSGE RIPIGAKIYV GRIGGSEAVF FLKDSRIAGG ATGDKEGKKY LAGAYIAYRK
DVPFYVWNDG AGANIKEGMV SLNRAAEGFF INALLSHRVS AKEFQSAIRS HNDLEVRKLC
DQLEKTLGWR FKAYQPEDRP KLCFVVAVGV GSSTGLDVYG SSQASLQVLL DEEQSYRVLT
GAAVIESVTG ETFTNYEIGG AKIMGRGTGT VDFVANDKLH LISYIRKIQS VLREVNNDPG
KLKIKNILKI RNSNSVEEII SESALASVSD AGEFLPIKAN YSGSESLVAG LLRFGGMPIT
VLGPRTEFGF HSFAALVKAK ETLRIAKKTG TGLLLVYGKK WFRSEYIEDS ESFRVRKDFQ
KSLQEFAEPL LHIVKDISGI SLTELSSVGD AWILVRPNRQ KNRGNDDALR QNSEMEKAAT
IVVDTDDEAY SKAASIFQLI HYRTIMDSGS TEKEPALPED PAKSYDMRHF LTESILDRDS
FVEFYAMDPG TSLVTGLGRI FGRTVGIIAD QPKDGGAPDA YGTDKFRVFM EFLNKYDISL
IMLSDAPGFV PGTKQERLRI QQIGGESLDV NVLSKNPVVS VVLRQNYGGR QIHAFSGFLR
PGISYYSWQS GTLAVMGAFS AFDLFQGAKV AKLEGEGKTL EIEKLRKEFL DSFKQKAEAS
NDALKSGVLD GVFGSISELR SVILNGLDSA AEKRRAWMEE KNGKPMEEVF SKSDTGVIG
//
