ID A0A073ITS1_9RHOB Unreviewed; 667 AA.
AC A0A073ITS1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acetyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:KEJ93728.1};
GN ORFNames=SUH3_16085 {ECO:0000313|EMBL:KEJ93728.1};
OS Pseudosulfitobacter pseudonitzschiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudosulfitobacter.
OX NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ93728.1, ECO:0000313|Proteomes:UP000027746};
RN [1] {ECO:0000313|EMBL:KEJ93728.1, ECO:0000313|Proteomes:UP000027746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KEJ93728.1,
RC ECO:0000313|Proteomes:UP000027746};
RA Lai Q., Hong Z.;
RT "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL Submitted (JAN-2014) 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:KEJ93728.1}.
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DR EMBL; JAMD01000030; KEJ93728.1; -; Genomic_DNA.
DR RefSeq; WP_037931792.1; NZ_WKFG01000014.1.
DR AlphaFoldDB; A0A073ITS1; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000027746; 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; 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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000027746}.
FT DOMAIN 2..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 585..662
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 667 AA; 70495 MW; 518602ADD048ED0F CRC64;
MSFSRVLIAN RGEIARRIQR GCRKLGLETV AVFSEADRDA PFVIEADHAV CIGGAAPSES
YLNVDAILDA ARVTGAGAVH PGYGFLSENA GFAAAVEAAG LVFIGPEPGA IAMMGSKIEA
KAAAEAAGVP VLPGYRGTDQ SDARLLEEAR ALGTPLLVKA SAGGGGRGMR LVTDLADAPE
AIASARSEAK GAFGDAAVFL ERYAPRARHV EVQVLGDSHR TLLHLGDRDC SLQRNHQKLI
EEAPAADLPE DLRDDMRAAA VRLAQSIDYR SAGTVEYLYD PSRGEYYFLE MNTRLQVEHP
VTEAITGIDL VEWQLRIARG EPLTLAQTDV RFDGHAIEVR IAAENPAENF RPETGRITLW
APPAGVRLDS GVAAGSVVGH HYDSMVAKLI VHAPDRAGAI RRAVAAIDTF AVGGVGLNLS
YQRALLTHAD FQALRHHTSG LPEMFPDGWT QPTPDTRDSG LAVMALHLHL APAGTSPWES
LGAWRLTAPG GRPGAASYWT TSLDDPIRIS GTPETLVAVL PDGQSLTTKT AAMTADRLSG
RVDGVPFTRI AHVERAGDHW RVHLQTPAGM TLTDLRTLED RHLARASVGA SGADLLTAPM
PGAVAEVRVA PGDTVAAGDT LVVLEAMKLL QSLPAPVAGV VTEIYCAPGD TVAGHAPLVK
LDPEEQT
//
