ID Q0BWF8_HYPNA Unreviewed; 920 AA.
AC Q0BWF8;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 123.
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:ABI77339.1};
GN OrderedLocusNames=HNE_3514 {ECO:0000313|EMBL:ABI77339.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI77339.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI77339.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI77339.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI77339.1; -; Genomic_DNA.
DR RefSeq; WP_011648479.1; NC_008358.1.
DR AlphaFoldDB; Q0BWF8; -.
DR STRING; 228405.HNE_3514; -.
DR KEGG; hne:HNE_3514; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000001959; 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:UP000001959}.
FT DOMAIN 80..589
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 719..843
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 408..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 99494 MW; FF54732DC1E0B454 CRC64;
MPSKDSFKSK STLTAAGKTY TYYSLEAAAK NGGLGDVSRL PAALKVLLEN MLRFEDGLTV
NEDDIRAFGE WADKGGQNPR EIAYRPARVL MQDFTGVPAV VDLAAMRDGI KALGGSAKKI
NPLVPVDLVI DHSVMIDEFG TPRAFQANVD LEYERNMERY TFLKWGQKAF NNFRVVPPGT
GICHQVNLEY LAQTIWSAPN EAGELVAYPD TLVGTDSHTT MVNGLAVLGW GVGGIEAEAA
MLGQPVSMLI PEVVGFKVTG AMTEGVTATD LVLKVVQMLR KHGVVNKFVE FYGPGLDNMP
LADRATIANM APEYGATCGF FPIDDETIRY LRQTGRDEDR IALVEAYAKQ NGFWRGADYA
PVYTSTLHLD LGDVVPAISG PKRPQDHVAL DAAAQVFGEY IHGLRKPAKA PELQKSEMTE
EGGAPAPASI PGDEMGPGRG RVDGQDYILN DGSVVIASIT SCTNTSNPYV LIGAGLVARK
ARALGLTRKP WVKTSLAPGS QVVSEYLNAA GLQEDLDALG FNLVGYGCTT CIGNSGPLAP
EISKSINEND LVAVSVLSGN RNFEGRISPD VRANYLASPP LVVAYAIAGD MNIDITKDAI
GTSKDGKPVY LKDIWPTTKE IADMVHATVT RQMFMSKYAD VFKGDEKWQG VQTTDAETYD
WPVSSTYIQN PPYFRGMSAE KGDIHPIKGA RVLALLGDMI TTDHISPAGS FKANSPAGKY
LTERQVPVKD FNSYGSRRGN HEIMMRGTFA NIRIKNEMLD GVEGGYTLGP DGEQTSIYDA
AMAWIDKGVP LVIIGGIEYG AGSSRDWAAK GTNLLGVKAV IAESFERIHR SNLVGMGVIP
FEFIGEGRKS LDLKGTETFD IEGLGNDIRP LSTVPCKITY ADGTVKTIQI KCRIDTEIEV
DYVKHGGVLH YVLRDLVRAS
//
