ID A1KYC7_CROS5 Unreviewed; 376 AA. AC A1KYC7; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 24-JUL-2024, entry version 60. DE RecName: Full=Homocitrate synthase {ECO:0000256|RuleBase:RU367143}; DE EC=2.3.3.14 {ECO:0000256|RuleBase:RU367143}; GN Name=nifV {ECO:0000313|EMBL:AAW56980.1}; OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain OS ATCC 51142)). OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica. OX NCBI_TaxID=43989 {ECO:0000313|EMBL:AAW56980.1}; RN [1] {ECO:0000313|EMBL:AAW56980.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 51142 {ECO:0000313|EMBL:AAW56980.1}; RX PubMed=18226230; DOI=10.1186/1471-2148-8-30; RA Kneip C., Voss C., Lockhart P.J., Maier U.G.; RT "The cyanobacterial endosymbiont of the unicellular algae Rhopalodia gibba RT shows reductive genome evolution."; RL BMC Evol. Biol. 8:30-30(2008). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY728386; AAW56980.1; -; Genomic_DNA. DR AlphaFoldDB; A1KYC7; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 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:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule. 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; 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; 40779 MW; B421AFC7A93507EA CRC64; MNHVHVNDTT LRDGEQAAGI VFSAIEKIAI ACLMDAIGIP ELEVGIPAMG GSEAESHHRH CPKRLKTALL GLEPCGSSDI EASIACGLRR VHISVPVSDI QIKAKFKGKT NLVWDRLRDS INFALDHDLF VSVGAEDASR ADESFLVEVA QFAESLGASR FRFCDTVGIL NPLTTAQKVG KLVKSIKMPI EMHTHNDFGL ATANALAGLQ AGAVSVNTTV NGLGERAGNA ALEEMIMALK RLYQVDLGME SSRLRELSQL VVKASGIPLP PWKAIVGTMF AHESGIHAHG VLQNPQTYEP FSPDEVGWKR RLVVGKHSGR HLLTNLLSQH GISLNHEESQ VVLDSVRHLS VQMKRSLTVE ELIDVVTNRS MSHGIV //