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Database: UniProt
Entry: A1Y9H7_9BACT
LinkDB: A1Y9H7_9BACT
Original site: A1Y9H7_9BACT 
ID   A1Y9H7_9BACT            Unreviewed;       432 AA.
AC   A1Y9H7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=ATP citrate lyase beta subunit {ECO:0000313|EMBL:ABI50079.1};
GN   Name=aclB {ECO:0000313|EMBL:ABI50079.1};
OS   Desulfurobacterium thermolithotrophum.
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Desulfurobacterium.
OX   NCBI_TaxID=64160 {ECO:0000313|EMBL:ABI50079.1};
RN   [1] {ECO:0000313|EMBL:ABI50079.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hugler M., Huber H., Molyneaux S.J., Vetriani C., Sievert S.M.;
RT   "Autotrophic CO2 fixation via the reductive tricarboxylic acid cycle in
RT   different lineages within the phylum Aquificae: evidence for two ways of
RT   citrate cleavage.";
RL   Environ. Microbiol. 9:81-92(2007).
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DR   EMBL; DQ853419; ABI50079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1Y9H7; -.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.30.470.110; -; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR032263; Citrate-bd.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF16114; Citrate_bind; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lyase {ECO:0000313|EMBL:ABI50079.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          42..214
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          253..429
FT                   /note="ATP-citrate synthase citrate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16114"
SQ   SEQUENCE   432 AA;  48899 MW;  9C455B55715480F4 CRC64;
     MAQKAIREYD GKRILAEHWN EYFAPEFEYD FKSVLVTPQT DLDKLPEEYP WLRELPLVAK
     PDMLFGKRGK LGLILFKKEK PCDVDYEAAK EWIKKKMEED VEIKGKKGKL THFLIEPCVP
     HAQEDEYYVA MTLGQDGDHI FMSAFGGIDV EENWDKVKEV VIPVLATDEE AEKLIEENVP
     EEIKDKEKYA DFVKRLYKFF KDMHFAYLEI NPLVMVGNKI YPLDFVGRLD DTAQFLVGRK
     WGEIEFPAGF GGELTPEEKY IKNGRKSGAS LKLTILNPEG RIWTLVAGGG ASVVYADTVA
     DLGYVNELAN YGEYSGNPSR AETREYVKTV LDFMTGKKDP QGRPKILIIG GAIANFTDVA
     KTFDGIIDAF KEYADKMKEV GVKIYVRHGG PNYEVGLARI KKAAEELGLP IEVYGPETHI
     TAIVKKALTE NP
//
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