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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//