ID W8VVS3_9FLAO Unreviewed; 755 AA.
AC W8VVS3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN ORFNames=NMS_0128 {ECO:0000313|EMBL:BAO54137.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO54137.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO54137.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO54137.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
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 -!- 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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; AP014548; BAO54137.1; -; Genomic_DNA.
DR RefSeq; WP_041494884.1; NZ_AP014548.1.
DR AlphaFoldDB; W8VVS3; -.
DR STRING; 1454201.NMS_0128; -.
DR HOGENOM; CLU_006714_2_2_10; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000031760; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd01584; AcnA_Mitochondrial; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 35..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..685
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 755 AA; 82409 MW; 511AD7CB85C441D0 CRC64;
MAFDIDMIKK VYETMPERVD KARELVGKPL TLSEKILYSH LWDGKAEKPF TRGKDYVDFA
PDRIACQDAT AQMALLQFMQ AGKSQVAVPT TVHCDHLIQA KQGASKDLAR ANDVSHEVFD
FLGSVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MVAIGVGGAD
AVDVMAGMAW ELKFPKLIGV KLTGKINGWT SAKDVILKVA GILTVKGGTG AIIEYFGEGA
KNLSCTGKGT ICNMGAEVGA TTSTFGYDES MSRYLRATDR ADIADEADKV AKYLTADDEV
YANPEQYFDQ VIEINLDELV PHLNGPFTPD LATPVGQLGE KAKENDWPLK VDWGLIGSCT
NSSYEDLTRA ASIAEQAVKK NIKPKSDFGI NPGSEQIRFT AERDGILKVF EDLDATIFTN
ACGPCIGQWD RSDAKGDAKN TIVHSFNRNF SKRADGNPNT HAFVGSPEMV AAIAISGRLD
FNPMTDKLIN EDGEEVMLDE PSGIELPPKG FEVEDAGYEA PVEDGSKVSV KVAEDSDRLQ
LLTPFEPWDG ENLMGAKLLI KAFGKCTTDH ISMAGPWLKY RGHLDNISNN CLIGAVNAFN
KQTNLVKSQI DGEYDAVPKT QRAYKKAGIP TVVVGDHNYG EGSSREHAAM EPRHLGVYVV
LVKSFARIHE TNLKKQGMLG VTFANESDYD LIQEDDTFNF VDLENFAPDQ PLTVELVHKD
GSKDTFKVNH TYNDAQIKWY RKGSALNLIK EENAA
//
