ID A0A0P8A6Z9_9CYAN Unreviewed; 390 AA.
AC A0A0P8A6Z9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:KPQ39029.1};
GN ORFNames=HLUCCO16_09800 {ECO:0000313|EMBL:KPQ39029.1};
OS Phormidium sp. OSCR.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=1666905 {ECO:0000313|EMBL:KPQ39029.1, ECO:0000313|Proteomes:UP000050461};
RN [1] {ECO:0000313|EMBL:KPQ39029.1, ECO:0000313|Proteomes:UP000050461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSCR {ECO:0000313|EMBL:KPQ39029.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KPQ39029.1}.
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DR EMBL; LJZT01000032; KPQ39029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8A6Z9; -.
DR STRING; 1666905.HLUCCO16_09800; -.
DR PATRIC; fig|1666905.3.peg.1649; -.
DR Proteomes; UP000050461; Unassembled WGS sequence.
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 Nitrogen fixation {ECO:0000256|RuleBase:RU367143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 15..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 390 AA; 42155 MW; A7A621A1B13BEF3A CRC64;
MKNCQTAVVR DPEPPRLLDT TLRDGEQMAG VALTGDEKVA IAQLLDAIGV PEIEVGIPAM
GGDEALAIST LVKSHLNAEL LGWNRAVISD LAASFNCGLQ RVHISLPVSE VQIAAKFGGD
RQRLWQQLHE SLNFARDRST FISVGAEDAS RADPDLLLAV AQTAQSLGAQ RFRFCDTVGI
LDPFEMMKQV QRLVHHLQIP VEVHTHDDLG MATANALAGL RAGASVVDVT VNGIGERAGN
AALEEVVMAM RRLQGWDFGI DSRQLLLLSR QVHQWMAGGT LPPWKAIVGD NAFAHEAGIH
ADAILKNPQT YEPFPPQWLG AEHQVRIGKH SGRRAIAACL AAQRIPDPGW GDRQELLDAV
RVRAIELKRG LAVEEVLALA ASSAPQTFPS
//
