ID A0A0R2VPQ0_9SPHI Unreviewed; 1634 AA.
AC A0A0R2VPQ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KRP13743.1};
GN ORFNames=ABR95_10880 {ECO:0000313|EMBL:KRP13743.1};
OS Sphingobacteriales bacterium BACL12 MAG-120813-bin55.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1655600 {ECO:0000313|EMBL:KRP13743.1, ECO:0000313|Proteomes:UP000050993};
RN [1] {ECO:0000313|EMBL:KRP13743.1, ECO:0000313|Proteomes:UP000050993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL12 MAG-120813-bin55 {ECO:0000313|EMBL:KRP13743.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRP13743.1}.
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DR EMBL; LICN01000013; KRP13743.1; -; Genomic_DNA.
DR Proteomes; UP000050993; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.70.20; -; 2.
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 PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF13370; Fer4_13; 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; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:KRP13743.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 778..808
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 911..940
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1634 AA; 182729 MW; 615C33DEFB794031 CRC64;
MDKHNNNVKY PGIRAAMDGN TAVIMCERES SDAAGAYPIT PSTQMGEYWA EEAAKGHLNI
SDRPLIFIEP EGEHAAAAVT AGLSMTGLRS ANFSSGQGIA YMHESLYAAV GKRLTYVLNI
GARAMTKSTL NVHAGHDDYH AIDDTGFFQL FAKNAQHAAD FNIIAHKVAE LSLTPGVVAQ
DGFLTTHLIE SLQVPERELI REFLGRPDDI IDTPTPAQRI IYGEQRRRIP ELWDVDNPMM
AGIVQNQDAY MQSVAAQRPF FFDHIQEIID NAFREFEGLT GRSYERVMTY RTEDADYLIL
GQGSIIPSAQ VVADYLRNTR KIKVGVVDLV MFRPFPADLI GKILKGKKGV AILERLDQPL
ASDLPIAREV RATLAKCLEN DGYKTGKPYP ALESYSQKDM PVIYSGSFGM GSRDLQPEGI
IGAVENMLPD GKHKKMFYLS IDFLRDAAFT PKQKAYQETI ADAYPQIKDL AIRGSENPNL
MPKGAITVRF HSVGGWGAIT TGKNLAMTLF DLLDYHIKAN PKYGSEKKGQ PTTYYLAAAP
EPIRVNCEYF FVDVVLSPDP NVFKHTNALA GLKEGGCFII QSERSKPEEV WNDIPRQYQQ
LIIDNNIRIF YIDGFRIARE EATDPELQLR MQGIAFQGAF FAASPVMQQA GLTDASLLKA
IEDQVKSKFG GKGQRVVDDN MRVVKRGFDE VHEIKNKVIS TDSGEKTNRQ TVLPLPTMLK
HMPQSASRLS DIHRFWEQTG NFYQRGMGND NITDPFIGLS VMPAASSLFR DMTGIRFEHP
EWIPNNCTAC GDCYTVCPDT AIPGLVSELS DVLNTIVTRV KKNHGEVNAL PKAVRQMESK
VRALFTSEKT DATVNDYIQE AIDQMLEENK DEQLAKEFKW FREELGDFRF ALTRPYFELH
EKDAPGSGGL FSITVNPTTC KGCMECVQVC NDDALRSVPQ TEASVARLRK EWDLWTDLPN
TPDQYKRIDD LEEKIGPLET LLLNKDAYLN FASGDGACLG CSEKSVIHLF VATVESLMQP
RVKKHIAYLT ELCDQLEKHI QGKLMGSVNV ADAAAIEKIT AEAHDHDLTM SELTQRLEQE
KGGTPIDQEW LREMTQLLAK LKQLKWKYTD GTTQKGRSSM GMCNATGCTS VWGSTWPYNP
YPFPWANHLF QDSTSMAMGI FEGHMSKMAD GFKVIRRAEM ELAGTYRAAD HKDFFTYFNW
QQFTDEEWHL CPPVVALGGD GAMYDIGFQN LSRLMASGKP VKVVVVDTQV YSNTGGQACT
SGFVGQISDM AQYGKVLQGK SEPRKEIGLI AMAHRNTYVM QATLANTSHM IEGFIDGLMT
RRPALFNLYT TCQPEHGVGD DMGVHQAKLA VESRAYPVFK FNPDNGITAR EGFDIEGNPA
MDQLWPTYRL QYKENGRTKT MEVAMTFADF ALTEARFRKH FRQVPKDSWN ENMVPLANFL
ELSEEEREGK YPYIWAVDRK QQLNRVLVAM KIVEACEERR NFWIMLRDIA GVKPAEEKQE
DIEGKIRAEV VGRIAKGLMQ LAGDDGNGIM QLVEEPEAKA AETASENGTS AASLAPWLET
ESCTACDECI KINPNIFAYN SDKKAYIKNP DGGPYQDLVK AAEKCTARVI HPGLPAQQTG
KDIEKWMTRA AKYN
//