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Database: UniProt
Entry: D3SR90_NATMM
LinkDB: D3SR90_NATMM
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ID   D3SR90_NATMM            Unreviewed;       611 AA.
AC   D3SR90;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Carbamoyl-phosphate synthaseATP-binding subunit L {ECO:0000313|EMBL:ELY31893.1};
DE   SubName: Full=Propionyl-CoA carboxylase biotin carboxylase component {ECO:0000313|EMBL:ADD06646.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:ADD06646.1};
GN   Name=pccA2 {ECO:0000313|EMBL:ADD06646.1};
GN   OrderedLocusNames=Nmag_3094 {ECO:0000313|EMBL:ADD06646.1};
GN   ORFNames=C500_04928 {ECO:0000313|EMBL:ELY31893.1};
OS   Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS   IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS   magadii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD06646.1, ECO:0000313|Proteomes:UP000001879};
RN   [1] {ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000001879};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA   Maupin-Furlow J.A., Woyke T.;
RT   "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADD06646.1, ECO:0000313|Proteomes:UP000001879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06646.1}, and ATCC 43099 / DSM
RC   3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC   NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX   PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA   Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA   Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA   Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT   "A comparative genomics perspective on the genetic content of the
RT   alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL   BMC Genomics 13:165-165(2012).
RN   [3] {ECO:0000313|EMBL:ELY31893.1, ECO:0000313|Proteomes:UP000011543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC   8861 / NBRC 102185 / NCIMB 2190 / MS3
RC   {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC   {ECO:0000313|EMBL:ELY31893.1};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4] {ECO:0000313|EMBL:ADD06646.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06646.1};
RA   Pfeiffer F.;
RL   Submitted (SEP-2016) 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; CP001932; ADD06646.1; -; Genomic_DNA.
DR   EMBL; AOHS01000023; ELY31893.1; -; Genomic_DNA.
DR   RefSeq; WP_004214632.1; NZ_AOHS01000023.1.
DR   AlphaFoldDB; D3SR90; -.
DR   STRING; 547559.Nmag_3094; -.
DR   PaxDb; 547559-Nmag_3094; -.
DR   GeneID; 8825954; -.
DR   KEGG; nmg:Nmag_3094; -.
DR   PATRIC; fig|547559.17.peg.942; -.
DR   eggNOG; arCOG01591; Archaea.
DR   HOGENOM; CLU_000395_3_1_2; -.
DR   OrthoDB; 31083at2157; -.
DR   Proteomes; UP000001879; Chromosome.
DR   Proteomes; UP000011543; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
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; PS50968; BIOTINYL_LIPOYL; 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, ECO:0000313|EMBL:ADD06646.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001879}.
FT   DOMAIN          1..460
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          121..330
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          533..611
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          468..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  66017 MW;  EEE1883DCD80EE28 CRC64;
     MFRKVLVANR GEIAVRVMRA CEELNVGTVA IYSEADKGSG HVRYADEAYN VGPARAADSY
     LDHEAVIEAA QKADADAIHP GYGFLAENAE FASKVEAADG ITWIGPSSDA MESLGEKTKA
     RQIMDEAAVP IVPGTTDPVT DPDEVAAFGD EHGYPIAIKA EGGGGGRGMK VVWDQSEIED
     QLESAKREGE AYFDNDSVYL ERYLEQPRHI EIQILADGHG NVRHLGERDC SLQRRHQKVI
     EEGPSAALSE ELREKIGEAA RRGVAAADYT NAGTVEFLVE EEPGRGPEEP LGPDANFYFL
     EVNTRIQVEH TVTEEITGID IVKRQIQIAA GEEVDFTQEE VDIDGHAMEF RINAENAAED
     FAPATGGTLE TYDPPGGVGV RMDDALRQGD ELVTDYDSMI AKLIVWGEDR EECIDRSLRA
     LSEYEIAGIP TIIPFHRLML TDEEFVASTH TTKYLDNELD ESRIEEAQEQ WGGDTGSGAS
     DDEETVEREF TVEVNGKRFE VELAEHGAPA IPVGDVDASG ASGPPQPAGG DSSGDDDIAG
     DGETVDAEMQ GTILDVAVEE GDEVAAGDVL VVLEAMKMEN DIVASRGGTV TEIAVEEEQS
     VDMGDTLVVL E
//
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