ID A0A078M5C4_9STAP Unreviewed; 903 AA.
AC A0A078M5C4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:CEA00547.1};
GN ORFNames=BN1048_00996 {ECO:0000313|EMBL:CEA00547.1};
OS Jeotgalicoccus saudimassiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Jeotgalicoccus.
OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CEA00547.1, ECO:0000313|Proteomes:UP000044136};
RN [1] {ECO:0000313|EMBL:CEA00547.1, ECO:0000313|Proteomes:UP000044136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13MG44_air {ECO:0000313|EMBL:CEA00547.1,
RC ECO:0000313|Proteomes:UP000044136};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-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 -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC the 2-methylcitrate cycle I (propionate degradation route). Catalyzes
CC the reversible isomerization of citrate to isocitrate via cis-
CC aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to
CC yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a
CC RNA-binding regulatory protein. {ECO:0000256|ARBA:ARBA00002737}.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CCSE01000001; CEA00547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078M5C4; -.
DR STRING; 1461582.BN1048_00996; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_9; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000044136; 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:0003723; F:RNA 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000044136};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 77..571
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 702..828
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 903 AA; 98811 MW; 129926B89B5B6721 CRC64;
MMSKNVKDNS RQTLSVNGKD YTYYSLQSLA DSGMSKSENL PYSIRVLLES VLRQYDGSVI
DDKHIEALAN WDKGDIKGKE VPFKPSRVIL QDFTGVPAVV DLASLRTAMD AVGGDVQKIN
PEVPVDLVID HSVQVDEYGS MNALQKNMDL EFERNMERYE FLRWATKAFD NYQAVPPATG
IVHQVNLEYL ANVVHEREEN GEPVLFPDTL VGTDSHTTMI NGLGVLGWGV GGIEAEASML
GQPSYFPVPE VIGVKMINAL PEGTTATDLA LRVTEELRKK GVVGKFVEFF GQGVTELPLA
DRATIANMAP EYGATCGFFA VDEETLDYLT LTGRDPEHVE VVREYLKANN LFFDAAVEPT
YTDVVELDLS TVESSLAGPK RPQDLINLSD MKEEYKKSVT APSGNHGHGL TEEEFDKTGT
VKYNDGEEQE LKTGDLVIAA ITSCTNTSNP YVMLGAGLIA KKAVEKGLTV PKYVKTSLAP
GSKVVTGYLE DAGLQPYLDQ LGFNLVGYGC TTCIGNSGPL RPEVTKTIVD NDMLVSSVLS
GNRNFEGRIH PLVKANYLAS PQLVVAYALA GTVDIDLRTE PLGKDKDGND VYMKDIWPSI
KEVRDTVMST VTPELFRKEY ETVFDSNETW NNIDVTDAPL YDFGDESTYI QNPSFFQNLS
KEAGTIEPLN GLRVLGKFGD SVTTDHISPA GAIGKDTPAG KWLIEQGVSP RDFNSYGSRR
GNHEVMVRGT FANIRIRNQI APGTEGGYTT YWPTGEVTSI YDASMKYQEE GTGLMVIAGD
DYGMGSSRDW AAKGTNLLGV KAVLAASYER IHRSNLVMMG VLPLQFVNGE NAEDHGLDGS
ESFDIQIDES VTAGEIIDVV ATKKNGDKVN LKAKVRFDSD VEADYYRHGG ILQLVLRKKI
ASA
//
