ID E6LXR8_9ACTO Unreviewed; 1673 AA.
AC E6LXR8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-binding domain protein {ECO:0000313|EMBL:EFU80435.1};
GN ORFNames=HMPREF0388_0655 {ECO:0000313|EMBL:EFU80435.1};
OS Mobiluncus curtisii ATCC 51333.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=887326 {ECO:0000313|EMBL:EFU80435.1, ECO:0000313|Proteomes:UP000005573};
RN [1] {ECO:0000313|EMBL:EFU80435.1, ECO:0000313|Proteomes:UP000005573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51333 {ECO:0000313|EMBL:EFU80435.1,
RC ECO:0000313|Proteomes:UP000005573};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:EFU80435.1}.
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DR EMBL; AEPY01000004; EFU80435.1; -; Genomic_DNA.
DR RefSeq; WP_004009080.1; NZ_GL622340.1.
DR HOGENOM; CLU_242773_0_0_11; -.
DR Proteomes; UP000005573; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF12837; Fer4_6; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:EFU80435.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 860..889
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 984..1013
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT COILED 1090..1117
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1519..1553
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1673 AA; 179188 MW; B673AA48C1EB9FB5 CRC64;
MVDQPKYPGK VEVINGNGAV ARVMNMVCGG VIGYPITPST EISETFEAAV AAGQKNVWGQ
HPFFFEPEGE HSAQSGAMGA ALTGGKFISN ASSSQGILYG LESHYVTVGK RIGGFVLQVA
ARVVSRHSLN VMGGHDDVYA LLPAGYTVLF GANPEEAANL ALISYRASSL SLIPVANCMD
GFATSHMMSE ARLPEAELVK EYLGDPKGYI PCPTAAQEIL FGAKGRAFQF GQFLESKRSV
LAPASLEALR SFLQSADNAE AIENDCYGEL FDREIAGHLP ATEVAKWRRQ WVNAPARGTR
KLIPSLVDID NPGLTGPVQN QPDFQAGVAD HHTHFVADVP RLVRQAMDEY NALTGSDYAP
VKTFNCEDAD FIMVGVGSIC EDVRAVLPYL RNRGLKVGLV QIVMLQPFPE ADLVAALKGA
KAVTVLERSD QAALTKFVNS ALVKAGQNAA AVQRDLPARY PNIAAVETGE MPQLSTGFFG
LGGHDVQPRH LIATFKAMQA GDLAPEFYIG STFFDDDATG EQKAMQDRLR EAYPETTKMA
LHLEENPKDL LPKEAMRIRF HSVGGYGTIA TGKLLADILA EMLHLHSKAA PKYGSEKSGA
ATNYYITLSP ETIRITNAEL EDVEIVVSPD HMVFAHTNPL KGLAEGGTFI LQSDKTPAEL
WASLPRRAKQ IIRDRHINLF ILDAFGVALK HAPNPGLQTR MMGVAFIGAI ATKVDRIASG
ASEADMLAKI REQIEHKFGA KGPAIVEANM AVVQDGAAAT QKVDWEQLDA DSAGGSAGAT
AGSGHSRPAL NASLSAAMCQ RGASGCALTS GLFDRDYFRR VVAEPFAQGT ISEAPVYPGT
GYFLPPASSA EKDKGLFRRT IPVFDPSVCT GCMECALACP DGAIPNTVFT IDTLLATAIE
QTGEAGASLQ SQVETIAGAM RQALLDTKAR PAIADVFTEV ATSQNADPAA VAAVADTLRT
FPVARTRPFF DSTEKRQPGA GVLFSATVDP WKCTGCLECV AVCGPHALIG TDQDEEVLDT
AQQRFAFLTK LPNSPSEFSD PNGGPSLDMK RIFLNRDNYY ATIGGHGACR GCGEVTAVRQ
TMALANDINN GRVLRHRQEL EELVAALEEK RHAVTDTALG ELIDQVRARL EQRLYRYEGP
AGGRGPAAAV VANSTGCSSV YASTAPFNPY QQPWVNGLFQ DAQPLAKGIY EGLAADLSMD
VLALRQARAI LAGATGAAIP NDAPEWKHFT DEELALMPAV MTIGGDGASY DIGFGAMSRI
MASGTPIKML VLNTGAYSNT GGQASTASLE GQDADLSRYG KYLKGKSEQR KELGLLAAMH
PNVLVVSTST AYQGHFLKNV SRALAQVDYP ALIDVYTPCQ PEHGIGDDMA SEHSRMAVKS
RVSPLFVHEP AHAEFSDRFI IDGNPDVKKL WSHYKLNYHD ADGKTQLLDL PYTPADFAYS
ELRFKKHFKP LPDNAENPTL VAEYIEMDAT ARETATPFIY TTGAEGNLVK IQVSPSIVKL
TEQCREYWTF LQYLAGQDLA AARKAQADLE KKLTETRDAA AKSQEEMIEL MAKAMAEVAA
TGTTTTPLPF LGGFGGGASS TGGASGSDAS GSAPAGSGTP FRYELEKIAQ CTDCKTCYQE
IPEYFEASTE IVDGKPTPVA RLIPGSLENV KVTDELRARI AKVVANCDAE IIS
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