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Database: UniProt
Entry: A0A147JCH4_9SPHN
LinkDB: A0A147JCH4_9SPHN
Original site: A0A147JCH4_9SPHN 
ID   A0A147JCH4_9SPHN        Unreviewed;       895 AA.
AC   A0A147JCH4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ORFNames=NS258_01690 {ECO:0000313|EMBL:KTW17600.1};
OS   Sphingomonas sanguinis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=33051 {ECO:0000313|EMBL:KTW17600.1, ECO:0000313|Proteomes:UP000074410};
RN   [1] {ECO:0000313|EMBL:KTW17600.1, ECO:0000313|Proteomes:UP000074410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS258 {ECO:0000313|EMBL:KTW17600.1,
RC   ECO:0000313|Proteomes:UP000074410};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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}.
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:KTW17600.1}.
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DR   EMBL; LDTC01000009; KTW17600.1; -; Genomic_DNA.
DR   RefSeq; WP_058715416.1; NZ_LDTC01000009.1.
DR   AlphaFoldDB; A0A147JCH4; -.
DR   PATRIC; fig|33051.5.peg.3629; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000074410; Unassembled WGS sequence.
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; CITRATE HYDRO-LYASE; 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|RuleBase:RU361275, ECO:0000313|EMBL:KTW17600.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          71..567
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          697..822
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   895 AA;  96864 MW;  9292E9FECD77376C CRC64;
     MTAIGQDSLN TRSTLDVDGK TYDYYSLAKA SEQLGDISRL PFSMKVLLEN LLRFEDGKTV
     TREDIQAIVD WQKTQRSDRE IQYRPARVLM QDFTGVPCVV DLAAMRDAIT KLGGDAAKIN
     PQVPVHLVID HSVMVDEFGT PQAFEDNVDL EYQRNMERYE FLKWGSKALD NFSVVPPGTG
     ICHQVNLEYI GQAIWSSTES GEHAKGGATI AYPDTLVGTD SHTTMINGLG VLGWGVGGIE
     AEAAMLGQPV SMLIPEVVGF KLTGKLQEGI TATDLVLTIT QMLRAKGVVG RFVEFYGPGL
     SSMTLADRAT IANMAPEYGA TCGFFPIDDK TLDYMRLTAR SDENVALVEA YAKANGFWRH
     DDAADPVFTD TLELDMSTVV PSLAGPKRPQ DKVVLTEVDD VFNADLAKVY KKDAAVRVAV
     EDRSHDIGDG DVVIAAITSC TNTSNPSVLV AAGLVARKAN ALGLKPKPWV KTSLAPGSQV
     VTDYLDKAGL TADLDAIGFN LVGYGCTTCI GNSGPLAEPI SKAINGNDIV AASVLSGNRN
     FEGRVSADVR ANFLASPPLV VAYALKGTVT QDMRETPIGQ GKDGQDVYLK DIWPSNDEVR
     SLMDANIDDE MFRSRYGNVY AGDAKWSAIE VTGSDTYAWP AASTYVANPP YFEGMEMTPK
     PVTDIIEAKP LAILGDSITT DHISPAGSIK ADSPAGTFLQ EHQVAKKDFN SYGARRGNHD
     VMMRGTFANI RIKNEMVPGV EGGMTQYEGE VMPIYDAAMR HKADGTPLVI VAGKEYGTGS
     SRDWAAKGTN LLGVRAVITE SFERIHRSNL VGMGVLPLQF ADGVTRETLK LDGSESFTIQ
     GVAGLRPRQD VEVILTRKDG STETFLTKCR IDTVNELEYF LNGGILQYVL RNLAA
//
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