ID D1NT47_9BIFI Unreviewed; 911 AA.
AC D1NT47;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:EFA23849.1};
GN ORFNames=BGLCM_0748 {ECO:0000313|EMBL:KFI59162.1}, BIFGAL_02958
GN {ECO:0000313|EMBL:EFA23849.1};
OS Bifidobacterium gallicum DSM 20093 = LMG 11596.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=561180 {ECO:0000313|EMBL:EFA23849.1, ECO:0000313|Proteomes:UP000003656};
RN [1] {ECO:0000313|EMBL:EFA23849.1, ECO:0000313|Proteomes:UP000003656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20093 {ECO:0000313|EMBL:EFA23849.1,
RC ECO:0000313|Proteomes:UP000003656};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFI59162.1, ECO:0000313|Proteomes:UP000029074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11596 {ECO:0000313|EMBL:KFI59162.1,
RC ECO:0000313|Proteomes:UP000029074};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
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 -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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:EFA23849.1}.
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DR EMBL; ABXB03000001; EFA23849.1; -; Genomic_DNA.
DR EMBL; JGYW01000004; KFI59162.1; -; Genomic_DNA.
DR AlphaFoldDB; D1NT47; -.
DR STRING; 561180.BIFGAL_02958; -.
DR eggNOG; COG1048; Bacteria.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000003656; Unassembled WGS sequence.
DR Proteomes; UP000029074; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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|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|RuleBase:RU361275, ECO:0000313|EMBL:EFA23849.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 66..572
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 702..834
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 911 AA; 99199 MW; AA8F08EDC209F25E CRC64;
MADHPQNGAE HMTLRESQLD TLTVGSTTFD YYRIADLAGI DHLPYSLKVL VENLVRNEDG
ANITDQHVQA LLDWDPAADP SHEIQFTPSR VVMQDFTGVP CVVDLATMRD AVKKLGGNPE
VINPQVQSDM IIDHSVQIDK YGVADAVEVN MDIEYQRNGE RYQFLRWGQQ AFENFRVVPP
GTGIIHQVNI EYLARVVMTK AQQDGNTLAY LDSCVGTDSH TTTVNGLGVL GWGVGGIEAE
AAMLGQPISM LVPRVVGFKL KGSIPEGVTA TDVVLTITDM LRQHGVVGKF VEFYGEGIAS
VPLANRATIG NMSPEFGSTC GIFPIDDVTL DYLRLTGRSD EQVELVKAYA KANKLWHDVN
DPDYVEPRYS EYLELDLSTV VPSIAGPKRP QDRIALSESK RVFEETLPGY VTDKTTREPV
AVSTDFRGDF ELTNGDVAIA SITSCTNTSN PSVMIAAGLL ARNAVARGLK PKPWVKTSLA
PGSQVVADYL QQAGLQDDLD ALGYQLVGFG CATCIGNSGP LLPEISEAIN TNDMTVTAVL
SGNRNFEGRI SPDVKMNYLA SPPLVIAYAL AGTMAFDFET EPLGQDGEGK PVFLKDIWPT
NEQVEQVVAD NVNREMFLKD YASVFDGDAR WKGLDVPEGE LFAWDPDSTY VRQQTFFDGM
TAQPAPVEDV RDARVLAFLG DSVTTDHISP AGAFKASSPA GQYLVEHGVQ QKDFNSYGSR
RGNHEVMVRG TFGNIRLRNL LLGAVGEEIT PGGYTYDFLE MKPTTIYEAS RNYIANDVPL
VVIGGKEYGT GSSRDWAAKG TAMLGVKAVI VESFERIHRS NLIGMGVLPL QFPEGESATS
LGLDGTETYS ITGITELNEG VTPKTVHVDA THADGSHTEF EAVVRIDTPG EADYYRNGGI
LQYVLRNLMK G
//
