ID A0A0R2R4N1_9FLAO Unreviewed; 755 AA.
AC A0A0R2R4N1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ABR79_03695 {ECO:0000313|EMBL:KRO55235.1};
OS Cryomorphaceae bacterium BACL11 MAG-121001-bin54.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655587 {ECO:0000313|EMBL:KRO55235.1, ECO:0000313|Proteomes:UP000051874};
RN [1] {ECO:0000313|EMBL:KRO55235.1, ECO:0000313|Proteomes:UP000051874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL11 MAG-121001-bin54 {ECO:0000313|EMBL:KRO55235.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRO55235.1}.
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DR EMBL; LIBL01000089; KRO55235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2R4N1; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000051874; Unassembled WGS sequence.
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 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};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 40..478
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..687
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 755 AA; 82196 MW; F645BC4826641E24 CRC64;
MAFDIEMIKK VYQKYPEAIQ AARKITKKPL TLAEKILYAH LWDGNATQEF KRGKDYVDFA
PDRVAMQDAT AQMALLQFMQ AGKSKVAVPS TTHADHLIQA KIGADKDLQE GINQNNEVFT
FLSSICNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLA MVAIGVGGAD
AVDVMAGMAW ELKFPKLIGV KLTGKLNGWT APKDVILKVA GILTVKGGTG AIVEYFGEGA
ISLSATGKGT ICNMGAEIGA TTSTFGYDKS MERYLRATDR DDVADAANEI KEHLTGDTEV
YANPEKYFDQ VIEINLDQLT PHLNGPFTPD LATQVGEMNE KATKNGWPLD IEWALIGSCT
NSSYEDLTRA ASIVEDAVNK GLKPKAILGI NPGSEQVRFT AERDGLIDIF NKFETTKIFT
NACGPCIGQW DREGADKKEK NSIVHSFNRN FAKRADGNPN THAFVGSPEM VAAIAISGRL
DFNPVTDTLT NQNGEQVKLA EPTGHELPPN GFAVEDNGYQ APAEDGSNIE VIVNSESNRL
QLLTPFKAWN GKNITGAKLL IKAEGKCTTD HISMAGPWLR YRGHLDNISN NCLIGAVNAF
TGKTNAVLNQ VNGKIDEVPN VARAYRAAGI TSIVVGDHNY GEGSSREHAA MEPRHLGVLA
VIVKSFARIH ETNLKKQGML GLTFANESDY DLIQEDDTFN FTDLADFKEG KKITLEVKHA
DKTIDIIMLN HSYNETQIDW FKAGSALNLI REQNS
//