ID Q7N4B7_PHOLL Unreviewed; 891 AA.
AC Q7N4B7;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN Name=acnA {ECO:0000313|EMBL:CAE14806.1};
GN OrderedLocusNames=plu2432 {ECO:0000313|EMBL:CAE14806.1};
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01) (Photorhabdus luminescens subsp. laumondii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265 {ECO:0000313|EMBL:CAE14806.1, ECO:0000313|Proteomes:UP000002514};
RN [1] {ECO:0000313|Proteomes:UP000002514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01
RC {ECO:0000313|Proteomes:UP000002514};
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023501,
CC ECO:0000256|RuleBase:RU361275};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; BX571867; CAE14806.1; -; Genomic_DNA.
DR RefSeq; WP_011146659.1; NC_005126.1.
DR AlphaFoldDB; Q7N4B7; -.
DR STRING; 243265.plu2432; -.
DR GeneID; 24166222; -.
DR KEGG; plu:plu2432; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002514}.
FT DOMAIN 69..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 691..818
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 891 AA; 98082 MW; BBE3F8182FD4299D CRC64;
MSFDLKKVCV STLSAASKQY DYYSLPLVAK HLGDISRLPK SLKVLLENLL RNIDGNSVVV
DDLKAIVDWQ NTGHADREIA YRPARVLMQD FTGVPAVVDL AAMREAVQRL GGNVEQVNPL
SPVDLVIDHS VMVDKFGTEK AFEQNVQLEM ERNYERYLFL RWGQKAFNRF RVVPPGTGIC
HQVNLEYLGK TVWHEMHNGR ELAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPDVV GFKLTGKLRE GITATDLVLT VTQMLRAHGV VGKFVEFYGD GLADLPLADR
ATIANMSPEY GATCGFFPAD GITLSYMRLT GRTEQQIELV EAYCKIQGLW RNPGDEPVFT
SSLELDMSTV EASLAGPKRP QDRVALARVP QVFQSSVDLE MNKSQGKAIS APVNLDNQKY
ELEEGAVVIA AITSCTNTSN PSVLMAAGLL AKKAVEKGLK RQPWVKTSLA PGSKVVTDYL
ELAGLMPYLE ELGFNLVGYG CTTCIGNSGP LPESIETAIK QADLTVGAVL SGNRNFEGRI
HPLIKTNWLA SPPLVVAYAL SGNMKKDLTK DPLGQDQQGN DVYLKDIWPD SKEIAKAVEQ
IKADMFHKEY AEVFDGDETW QSLDVASSAT YHFQLDSTYI RHPPFFSEMT AEPEAITDIH
GANILAILGD SVTTDHISPA GNIKADSPAG RYLQEHGVEP KDFNSYGSRR GNHEVMMRGT
FANIRIRNEM IAGVEGGYTR HIPSQTQLAI YDAAMRYQEE KTPLAIIAGK EYGSGSSRDW
AAKGTRLLGV RVVIAESFER IHRSNLIGMG VLPLEFPQGV NRKTLNLQGD ETIDIEGMNN
LKPGQIVPVK MTYSDGHQEI INAQCRIDTK TELDYFHHGG ILHYVIRHML K
//
