ID W6FWL9_NODSP Unreviewed; 376 AA.
AC W6FWL9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Homocitrate synthase {ECO:0000256|RuleBase:RU367143};
DE EC=2.3.3.14 {ECO:0000256|RuleBase:RU367143};
GN ORFNames=NSP_40540 {ECO:0000313|EMBL:AHJ30354.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ30354.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ30354.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ30354.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
CC -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
CC {ECO:0000256|RuleBase:RU367143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA +
CC H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58884; EC=2.3.3.14;
CC Evidence={ECO:0000256|RuleBase:RU367143};
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP007203; AHJ30354.1; -; Genomic_DNA.
DR RefSeq; WP_017804298.1; NZ_CP007203.1.
DR AlphaFoldDB; W6FWL9; -.
DR STRING; 313624.NSP_40540; -.
DR GeneID; 78019345; -.
DR PATRIC; fig|313624.11.peg.4069; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_4_2_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
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 NCBIfam; TIGR02660; nifV_homocitr; 1.
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:AHJ30354.1};
KW Nitrogen fixation {ECO:0000256|RuleBase:RU367143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 4..255
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 376 AA; 40816 MW; F25B5D1D20C381CB CRC64;
MNEILINDTT LRDGEQAAGV AFTFEEKVAI AQFLDAIGVP ELEVGIPAMG EAETHAILAI
SDLGLQASLL GWNRAVLSDI KASITCGLKR VHIAIPVSGI QIAAKFHGQW RVSLQRLKDC
ISFAVDQGLW VAVGGEDSSR ADPNFLLDVA LNAQEWGASR FRFCDTVGVL DPFSTYAKVK
QLVSALSIPL EIHTHNDFGL ATANALAGIK AGATSVNTTV NGVGERAGNA ALEEVVMSIK
RIYGINLGID TRRLLELSQL VASASNCHVP PWKAIVGENT FAHESGIHAH GVLQNPLTYE
PFAPEEVGWE RRLVVGKHSG RHLVTSLLQQ NDIFLNPEET QSVLDAVRQQ SVKQKRNLTV
EELLNLVREQ RYSHAT
//
