NIFV1_NOSS1
ID NIFV1_NOSS1 Reviewed; 377 AA.
AC Q44290;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Homocitrate synthase 1;
DE EC=2.3.3.14;
GN Name=nifV1; Synonyms=nifV; OrderedLocusNames=alr1407;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9139910; DOI=10.1128/jb.179.9.2930-2937.1997;
RA Stricker O., Masepohl B., Klipp W., Boehme H.;
RT "Identification and characterization of the nifV-nifZ-nifT gene region from
RT the filamentous cyanobacterium Anabaena sp. strain PCC 7120.";
RL J. Bacteriol. 179:2930-2937(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
CC -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
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 -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68174.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X99902; CAA68174.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BA000019; BAB73364.1; -; Genomic_DNA.
DR PIR; AD1982; AD1982.
DR RefSeq; WP_010995579.1; NZ_RSCN01000040.1.
DR AlphaFoldDB; Q44290; -.
DR SMR; Q44290; -.
DR STRING; 103690.17130754; -.
DR EnsemblBacteria; BAB73364; BAB73364; BAB73364.
DR KEGG; ana:alr1407; -.
DR eggNOG; COG0119; Bacteria.
DR OMA; SNMFAHE; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000002483; Chromosome.
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:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd07939; DRE_TIM_NifV; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013477; NifV/FrbC.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR02660; nifV_homocitr; 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; Reference proteome; Transferase.
FT CHAIN 1..377
FT /note="Homocitrate synthase 1"
FT /id="PRO_0000140456"
FT DOMAIN 4..255
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT CONFLICT 99..103
FT /note="GIQIA -> DVK (in Ref. 1; CAA68174)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> L (in Ref. 1; CAA68174)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="Q -> L (in Ref. 1; CAA68174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 40851 MW; 7FB0C6706875AA0A CRC64;
MNKVLINDTT LRDGEQAAGV VFTLEEKVAI AKFLDTIGVP ELEVGIPAMG EEEMRAICAI
SNLGLKANLL AWNRAVISDI KASVACGMER VHIAIPVSGI QIAAKFHGQW RVSLQRLKDC
ISFAVDQGLW VAVGGEDSSR ADENFLLDVA LYAQEWGASR FRFCDTVGVL DPFTTYGKVK
LLVSALTIPV EVHTHNDFGM ATANALAGIK AGASSVNTTV IGLGERAGNA ALEEVVMAIK
RIYGVDMGID TPRLLELSQL VAAASGANVP PWKAIVGENT FAHESGIHAH GVLQNPDTYE
PFAPEEVGWE RRLVVGKHSG RHSVSNLLEQ HGIFLNPEET QSVLDAVRQQ SIKKKRSLTT
EELLNLVKEQ RYSHAAR