ID Q0AVA6_SYNWW Unreviewed; 884 AA.
AC Q0AVA6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Putative flavoprotein {ECO:0000313|EMBL:ABI69348.1};
GN OrderedLocusNames=Swol_2054 {ECO:0000313|EMBL:ABI69348.1};
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI69348.1, ECO:0000313|Proteomes:UP000001968};
RN [1] {ECO:0000313|Proteomes:UP000001968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
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DR EMBL; CP000448; ABI69348.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0AVA6; -.
DR STRING; 335541.Swol_2054; -.
DR KEGG; swo:Swol_2054; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_017490_2_0_9; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000001968; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR CDD; cd07709; flavodiiron_proteins_MBL-fold; 1.
DR CDD; cd00729; rubredoxin_SM; 2.
DR Gene3D; 2.20.28.10; -; 2.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR045761; ODP_dom.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR041575; Rubredoxin_C.
DR InterPro; IPR048574; RUBY_RBDX.
DR PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR PANTHER; PTHR32145:SF11; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF19583; ODP; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR Pfam; PF21349; RUBY_RBDX; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 2.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001968}.
FT DOMAIN 267..405
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 417..451
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
FT DOMAIN 849..883
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 884 AA; 98400 MW; 22F8A48CB3561DB6 CRC64;
MAENYSKGGM LVKALEIKEN VFYVGVQDYD LRVFDIVMRT EYGTSYNAYL VKGREKTVLV
ETVKDKFFDE YIKDLQEIVK LSEIDYLIMN HTEPDHSGSV EKLLELIPGL TILGSQTAIR
FLKEISNKNF SSRELNHGDE LDLGGKTLRF ISAPFLHWPD SMYSYLPEDK ILFTCDSFGS
HYADEKVFND LIDFDFTDAY KYYFDMIMGP FKPYVLEALE KIKDLEFDVI CPGHGPVLRQ
NLDYYIELYR QWSTPVEVAE GEKKPSIVLA YVTAYGYTEM IADSLLEGIS MMGDFDIKRY
NLVEGGLEEV LQSIDQADGL LVGSPTINGD ALPPIWDLIT RLSPITHSDK VALAFGAYGW
SGEAVPSIES RLNALRMKVL PGFRVNFKPS ARQLEDAFTL GMEFARAVME KGQDKSKIRW
RCLVCGHIHV GEEPPAICPA CGVGPENFVQ MPLEDEFLND TSEHFVIIGS GIAALSAAQA
IRQRNRTAAI TMLTEEEALP YYRPALSDFL GEDLPDKRLY VFNAAWYQEN AIEVKTGFKV
NSIDTAARKV SGDNGENLTY NKLIVASGAR SNIPPFPGVE KEGVFALRNL KDAIKLKEAI
KTSKKAVVIG GGVLGLEAVW EMVSAGLEVS VVEFGERLMP RQLDDSSSAR LADIIRSKGV
QLYLGKATEE ILGEARASGV RLNDGQVLEA DLVLLSTGVK PNVELAQEAG LEIKQGIVVD
EKMRSSVPDV YAAGDVAQHG ERMIGLWPIA MEMGRIAGAA AAGDWLEYKE PRISTMLVAF
DKEIFSIGEV NLPPEQCRVV EVKDPIEDYY KKSFIKDGVL VGEIIIASWV DSSESVQKLG
RDKSGKQRHN RWKCRLCGYI HEGPEPPDIC PVCGAPKDMF DPID
//
