ID Q4FL10_PELUB Unreviewed; 889 AA.
AC Q4FL10;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
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:AAZ22128.1};
GN OrderedLocusNames=SAR11_1324 {ECO:0000313|EMBL:AAZ22128.1};
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ22128.1, ECO:0000313|Proteomes:UP000002528};
RN [1] {ECO:0000313|EMBL:AAZ22128.1, ECO:0000313|Proteomes:UP000002528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ22128.1,
RC ECO:0000313|Proteomes:UP000002528};
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ22128.1; -; Genomic_DNA.
DR RefSeq; WP_011282307.1; NC_007205.1.
DR AlphaFoldDB; Q4FL10; -.
DR STRING; 335992.SAR11_1324; -.
DR KEGG; pub:SAR11_1324; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000002528; 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:UP000002528}.
FT DOMAIN 79..559
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 695..816
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 889 AA; 98905 MW; 6FAA9F0814A0E5D1 CRC64;
MKPGNQNSYN SLKTISINDR DYKYYSLVEA EKNGLDGISK LPKSLKVLLE NLLRYEDDLS
VTKSQIEAIK EWLKTKKSLT EIAYRPARVL LQDYTGIPAV ADLAAMREAV KEKNKDPNTI
NPLSAVDLVI DHSVQVDKSA NSDSFEKNVD IEFKRNGERY SFLKWGQQAF NNFRIVPPGT
GICHQVNLEY LSKVVWSEKF QNEDYLFPDT LVGTDSHTTM VNGLSVLGWG VGGIEAEAGM
LGQPISMLIP EVIGFEVKNK MPEGTTATDL VLTVVKMLRD KGVVGKFVEF YGEGLKNLTL
ADRATIANMA PEYGATCGFF PIDEETLKYL RFSGRDENTV NIVENYAKEQ GLWANDQVEF
TDTLSLDMST VVPTISGPKR PQDKVLLTDA STGFKKVFED ATNRKEQHIS KVSGTDYEIK
DGSILIAAIT SCTNTSNPNV LIGAGLLAKK AVELGLETKP WVKTSLAPGS QVVTDYLAKA
GLNVFLDKLG FNLVGYGCTT CIGNSGPLPE EIVKAIDKEN IYAVSVLSGN RNFEGRISPH
IKANYLASPP LVVAYALAGH MEFDLYKEPL GKSKDGKDIF LKDIWPSNKE IEDTLRESLN
AEMFVKRYSN VSEGPKQWQE IKTENTSIYN WDSSSTYVKK PPFFENLSDQ PEGFKPIKEA
RPLLILGDMV TTDHISPAGN IQKESPTGEY FMEHQILPTD YNSYGSRRGN HEVMMRGTFA
NIRIRNEMAP GTEGGFTKLY PEEKVMPVYN AVEEYKKRGT DLVVIGGKEY GTGSSRDWAA
KGTKLLGVKV VIAESFERIH RSNLIGMGVL PLQFTEGHDR VNLKLIGSEL ITVLQIEDGI
NASDHVQVEI KYASGDIKKI KTLCRIDTKN ELEYYKNGGI LQYVLRNMI
//
