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Database: UniProt
Entry: R9GRF6_9SPHI
LinkDB: R9GRF6_9SPHI
Original site: R9GRF6_9SPHI 
ID   R9GRF6_9SPHI            Unreviewed;       383 AA.
AC   R9GRF6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Homocitrate synthase {ECO:0000313|EMBL:EOR94273.1};
DE            EC=2.3.3.14 {ECO:0000313|EMBL:EOR94273.1};
GN   ORFNames=ADIARSV_2514 {ECO:0000313|EMBL:EOR94273.1};
OS   Arcticibacter svalbardensis MN12-7.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR94273.1, ECO:0000313|Proteomes:UP000014174};
RN   [1] {ECO:0000313|EMBL:EOR94273.1, ECO:0000313|Proteomes:UP000014174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN12-7 {ECO:0000313|EMBL:EOR94273.1,
RC   ECO:0000313|Proteomes:UP000014174};
RX   PubMed=23846277;
RA   Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA   Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT   Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT   Sample.";
RL   Genome Announc. 1:E00484-13(2013).
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523}.
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:EOR94273.1}.
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DR   EMBL; AQPN01000090; EOR94273.1; -; Genomic_DNA.
DR   RefSeq; WP_016195745.1; NZ_AQPN01000090.1.
DR   AlphaFoldDB; R9GRF6; -.
DR   STRING; 1150600.ADIARSV_2514; -.
DR   PATRIC; fig|1150600.3.peg.2487; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9804858at2; -.
DR   Proteomes; UP000014174; Unassembled WGS sequence.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd07939; DRE_TIM_NifV; 1.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013477; NifV/FrbC.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR   PANTHER; PTHR42880:SF1; ISOPROPYLMALATE_HOMOCITRATE_CITRAMALATE SYNTHASE FAMILY PROTEIN; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:EOR94273.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014174};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          10..261
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   383 AA;  41809 MW;  7E9B050C9A836F08 CRC64;
     MGNDRGIFNT LLIDTTLRDG EQAPGVVFDL NDKIRIACLL EQAGIKEVEL GTPVMGSREV
     NDIKTIVELG LNFRSTAWCR ANRLDLDAAL KTGVNSVNIS FPVSPILLKA LGKNYHWVIE
     NLRDLVRYAS DHFEYIAIGA QDASRAEFSF LSYFLAEANR VGASRLRIAD TVGLLTPLST
     MELFTKVRKI LPDVSLEFHG HNDLGMATAN TLTALQTGAD AASLTVNGLG ERAGNAALEE
     LVMALDLGGK MEHGIHTEVL NELCMEVSKA SGIPIHDHKA ITGSKVLSHE SGIHTSCLLA
     NRETYQIIDP EKIGRPQGEF VFGKHSGTAA LISFLNSKAI AINKAESVSL LHVIKEMSCR
     LKRSLSQLEV QNLYLNKEYV INS
//
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